The most recent information on MAPK8 is here. Click here for the function of MAPK8. Edit this page in Wiki Genes - MAPK8 or see Wiki Gene. In addition, XIAP, NAIP, and JNK1 bind to TAK1. Paper-9195765. MEKK1/ JNK signaling stabilizes and activates p53. Paper-1558938. Thus, ASK1 is a mediator of TRAF2- induced JNK activation. Paper-1597944. The PEA-15 protein regulates autophagy via activation of JNK. Paper-15203271. However, MKP-2 is surprisingly only able to deactivate JNK in vivo. Paper-10995986. We also observed that DSCAM activates both JNK and p38 MAP kinases. Paper-10492022. Knockdown of ANP32A expression further induced p38 SAPK and COX-2. Paper-15348188. The amount of p53- JNK complex was inversely correlated with p53 level. Paper-1563237. JNK1 phosphorylates SIRT1 and promotes its enzymatic activity. Paper-14619807. The c-jun N-terminal kinase JNK1 interacts with WWOX and inhibits apoptosis. Paper-12965544. Akt2 negatively regulates assembly of the POSH-MLK- JNK signaling complex. Paper-10041354. Also, JNK1 blocked WOX1 prevention of cell cycle progression. Paper-9880509. Furthermore, p38(MAPK), ERK1/2, JNK, and Smad1 were phosphorylated by BMP4. Paper-10760113. Increased expression of NSP1 in 293 cells induces activation of JNK1, but not of ERK2. Paper-1812264. Moreover, JNK1 stimulated whereas SP600125 suppressed XAF1 promoter activity. Paper-13522880. In this study we elucidated the role of nonactive JNK in regulating p53 stability. Paper-1563237. Furthermore, restoration of JNK1 in ARMS reestablished a tumor-suppressive function for ILK. Paper-13815125. TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-beta. Paper-12958285. Anthocyanins also decreased activation of JNK and p38 induced by CD40. Paper-13075572. JNK targets p53 ubiquitination and degradation in nonstressed cells. Paper-1563237. The dual specificity JKAP specifically activates the c-Jun N-terminal kinase pathway. Paper-9171289. Significantly, Ha-Ras partially activates JNK1 and potentiates the activation caused by UV. Paper-115736. Therefore, JNK is differentially regulated by MKK4 and MKK7 depending on the stimulus. Paper-12913383. On the other hand, JNK and p38 mitogen- activated protein kinases were activated by TAK1. Paper-13406987. CONCLUSION: JNK1 promotes cell survival in Her2/neu-positive breast cancer. Paper-15396452. TNF-alpha activates MUC2 transcription via NF-kappaB but inhibits via JNK activation. Paper-10736785. Over-expression of TAO2 activated endogenous JNK/ SAPK and p38 but not ERK1/2. Paper-8778623. Herein we provide evidence that MLK3 can be phosphorylated by JNK in vitro and in vivo. Paper-12060573. JNK1 was preferentially activated in human breast cancer tissue overexpressing Her2/neu. Paper-15396452. Furthermore, knockdown of NFAT3 enhanced Ras- JNK1 or JNK2-induced foci formation in NIH3T3 cells. Paper-12496586. Promoter activity was induced by the JNK inhibitor SP600125 and was repressed by activated MEKK1. Paper-10825893. JNK1 binds to the c-Jun transactivation domain and phosphorylates it on Ser-63 and Ser-73. Paper-115736. Costimulation with or without IL-25 treatment could activate JNK, p38 MAPK and NF-kappaB. Paper-12557038. These MKK isoforms did not activate the ERK subgroup of MAP kinases, but MKK4 did activate JNK. Paper-157943. However, the subsequent steps in TRAF2- induced SAPK and NF-kappaB activation remain unresolved. Paper-1274354. Dual role of JNK1- mediated phosphorylation of Bcl-2 in autophagy and apoptosis regulation. Paper-13003478. Thus, the assembly of an active JNK signaling complex by POSH is negatively regulated by Akt2. Paper-10041354. JNK inhibition with SP600125 also blocked binding of Sp1 to the DR5/ TRAIL-R2 promoter. Paper-10287042. In both mouse and human cells, loss or reduction in JNK1 expression represses RNA pol III transcription. Paper-13926094. AMPK knockdown or mTOR overexpression impaired RSV- induced autophagy but not JNK activation. Paper-14232612. TGF-beta1 activated p38 alpha and JNK1, which initiated the phosphorylation of p21. Paper-9167971. Transient overexpression of NIK specifically activates the stress-activated protein kinase ( SAPK) pathway. Paper-989267. Thymosin beta-10 is aberrantly expressed in pancreatic cancer and induces JNK activation. Paper-13667559. Regulation of the orphan receptor TR3 nuclear functions by c-Jun N terminal kinase phosphorylation. Paper-12379283. Thus, JNK represses hTR promoter activity and expression, apparently by enhancing repression through Sp3. Paper-10825893. Sustained JNK1 activation is associated with altered histone H3 methylations in human liver cancer. Paper-13577715. Thus, activation of PARs but not stimulation with LPS leads to ERK1/2 and JNK- mediated production of IL-8. Paper-12682622. Hypoxia-induced bFGF gene expression is mediated through the JNK signal transduction pathway. Paper-2157708. Release of RASSF1C from the nucleus by Daxx degradation links DNA damage and SAPK/ JNK activation. Paper-12073843. Long form of cellular FLICE-inhibitory protein interacts with Daxx and prevents Fas- induced JNK activation. Paper-10084034. TRPM7 activates m-calpain by stress-dependent stimulation of p38 MAPK and c-Jun N-terminal kinase. Paper-14644928. The apoptosis signal-regulating kinase 1 ( ASK1) is activated by TNF and stimulates JNK activation. Paper-1597944. In addition, recombinant SCCA1 suppressed kinase activity of JNK1 but did not affect JNK2 or JNK3 kinase activity. Paper-12174800. Overexpression of MKP-1 in DU145 cells blocked activation of stress-activated protein kinase ( SAPK/ JNK). Paper-8346938. The JNK inhibitor SP600129 enhances apoptosis of HCC cells induced by the tumor suppressor WWOX. Paper-12965544. A kinase-inactive mutant NIK blocked CD27-, TRAF2-, and TRAF5- mediated NF-kappaB and SAPK/JNK activation. Paper-1453876. Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation. Paper-9628596. A peptide corresponding to the JNK binding site on p53 efficiently blocked ubiquitination of p53. Paper-1563237. Knockdown of either JNK1 or JNK2 with small interfering RNA also significantly reduced the regulated PTX3 expression. Paper-11281687. Sequential activation of protein kinase C delta and JNK is required for interferon-alpha- induced expression of IFIT4. Paper-14331818. JunB-control of IL-4 expression is mediated by the phosphorylation of JunB at Thr102 and -104 by JNK MAP kinase. Paper-1752293. The activation of JNK is substantially inhibited by siRNA- mediated down-regulation of endogenous PEA-15. Paper-15203271. We showed that TOPK associated with and phosphorylated JNK1 following UVB irradiation in vitro or in vivo. Paper-13263824. Filamin associates with stress signalling kinases MKK7 and MKK4 and regulates JNK activation. Paper-14686837. In conclusion, our data show that PEA-15 promotes autophagy in glioma cells in a JNK-dependent manner. Paper-15203271. Prostate-derived sterile 20-like kinase 2 ( PSK2) regulates apoptotic morphology via C-Jun N-terminal kinase and Rho kinase-1. Paper-11311369. CONCLUSION: JNK1 is associated with UV signal transduction in human epidermis and SCCA1 is a suppressor of this process. Paper-12174800. Repression by MEKK1 was blocked by SP600125 or enhanced by coexpression of wild-type but not phosphoacceptor mutated JNK. Paper-10825893. Redox-dependent matrix metalloproteinase-1 expression is regulated by JNK through Ets and AP-1 promoter motifs. Paper-12004952. Mixed lineage kinase-3/ JNK1 axis promotes migration of human gastric cancer cells following gastrin stimulation. Paper-14179543. Overexpressed TRAF2 or TRAF6 activate JNK, p38, or IKK in the absence of extracellular stimulation. Paper-1875239. This regulatory mechanism between JNK and Cdh1 reveals an important function for JNK during the cell cycle. Paper-15276637. Androgen via p21 inhibits tumor necrosis factor alpha- induced JNK activation and apoptosis. Paper-14157258. Axin utilizes distinct regions for competitive MEKK1 and MEKK4 binding and JNK activation. Paper-9989017. We noted that ASK1 and JNK1 were normally activated at G(2)/M phase, and JNK was capable of phosphorylating BCL-2. Paper-2050254. JNK regulates cell migration through promotion of tyrosine phosphorylation of paxillin. Paper-13036030. Moreover, UVB-induced JNK1 activity was greatly augmented in mouse epidermal JB6 Cl41 cells that stably expressed TOPK cDNA. Paper-13263824. Here we show that JSAP1 bound ASK1 and enhanced ASK1- and H(2)O(2)- induced JNK activity. Paper-9173055. Control of TrkA- induced cell death by JNK activation and differential expression of TrkA upon DNA damage. Paper-15374746. JSAP1 (also termed JIP3) is a scaffold protein that interacts with specific components of the JNK signaling pathway. Paper-9173055. In particular, c-Jun amino-terminal kinase ( JNK) was important for neurite outgrowth stimulated by both Wnt-3a and Dkk1. Paper-14292373. These results were mimicked by the JNK inhibitor SP600125, indicating that JNK can directly phosphorylate IRF3. Paper-12913383. Together, our data suggest that PS1 inhibits the stress- activated signaling by suppressing the SAPK/JNK pathway. Paper-8787641. Phosphorylation of Pax2 by the c-Jun N-terminal kinase and enhanced Pax2-dependent transcription activation. Paper-9154193. The c-Jun N-terminal kinase (JNK) phosphorylates the glucocorticoid receptor ( GR) and inhibits GR-mediated transcription. Paper-9628596. For this reason, MKK4 and MKK7 together produce a synergistic increase in the activity of each SAPK1/JNK isoform in vitro. Paper-8647530. CD99 costimulation up-regulates T cell receptor- mediated activation of JNK and AP-1. Paper-10949644. Our results suggest that cellular functions previously attributed to SAPK1 and/or SAPK2 may be mediated by SAPK3 or SAPK4. Paper-1091705. A catalytically inactive mutant of ASK1 is a dominant-negative inhibitor of TNF- and TRAF2- induced JNK activation. Paper-1597944. The importance of the JNK pathway for the regulated PTX3 expression may be a potential target for its regulation in the lung. Paper-11281687. We conclude that endogenous SOCS3 inhibits AP-1 activity through blocking of JNK phosphorylation. Paper-14343694. Inhibition of MITF and tyrosinase by paeonol- stimulated JNK/ SAPK to reduction of phosphorylated CREB. Paper-14315983. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Paper-115736. HIP-55 activates HPK1 and c-Jun N-terminal kinase (JNK), which are two important lymphocyte signaling molecules. Paper-10042597. Finally, interference with GCKR expression impeded TRAF2- and TNF- induced SAPK activation but not that of NF-kappaB. Paper-1274354. The activated JNK1 physically interacted with the phosphorylated WOX1, as determined by co-immunoprecipitation. Paper-9880509. Mammalian sterile 20-like kinase 3 ( MST3) mediates oxidative-stress- induced cell death by modulating JNK activation. Paper-13992823. A novel c-Jun N-terminal kinase (JNK)- binding protein WDR62 is recruited to stress granules and mediates a nonclassical JNK activation. Paper-14198757. In vitro phosphorylation of p53 by JNK abolished Mdm2 binding and targeting of p53 ubiquitination. Paper-1558938. Co-transfection of a dominant negative TRAF2 or TRAF5 blocked NF-kappaB and SAPK/JNK activation induced by CD27. Paper-1453876. Similarly, JNK1 was found to control the proliferation of human HCC cells by affecting p21 and c-Myc expression. Paper-14342042. The N-CoR- HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2. Paper-9202254. Our results revealed that adrenomedullin induced the phosphorylation of both c-Jun and JNK in glioblastoma cells. Paper-13616281. BACKGROUND/AIMS: Aberrant c-Jun N-terminal kinase (JNK) activation has been linked to hepatocellular carcinoma ( HCC) in mouse models. Paper-13577715. JNK regulates HIPK3 expression and promotes resistance to Fas-mediated apoptosis in DU 145 prostate carcinoma cells. Paper-10249300. Finally, the JNK1 was activated more efficiently in the MEKK2- JNKK2- JNK1 complex than was the JNK1 excluded from the complex. Paper-2149787. Glutathione S-transferase P1-1 ( GSTP1-1) inhibits c-Jun N-terminal kinase ( JNK1) signaling through interaction with the C terminus. Paper-8986561. Ectopic expression of PS1 in MEF(PS1(-/-)) cells suppressed H(2)O(2)- stimulated SAPK/JNK activity and apoptotic cell death. Paper-8787641. DAP kinase regulates JNK signaling by binding and activating protein kinase D under oxidative stress. Paper-12576070. Interacting JNK- docking sites in MKK7 promote binding and activation of JNK mitogen-activated protein kinases. Paper-11845266. Moreover, Gemin5 promoted the binding of ASK1 to SEK1 and to JNK1, as well as the ASK1- induced activation of JNK1. Paper-13341457. SOCS3 suppresses AP-1 transcriptional activity in neuroblastoma cells through inhibition of c-Jun N-terminal kinase. Paper-14343694. Furthermore, expression of the cytoplasmic domain of DSCAM induces a morphological change in cultured cells that is JNK-dependent. Paper-10492022. JNK1, JNK2, and JNK3 are involved in P-glycoprotein- mediated multidrug resistance of hepatocellular carcinoma cells. Paper-15148595. Interleukin-6 inhibits Fas- induced apoptosis and stress-activated protein kinase activation in multiple myeloma cells. Paper-828338. This process can be mitigated by enhancing Gadd45beta expression or by inhibiting the activity of JNK or its upstream regulator, MKK-7. Paper-14092777. Here we demonstrate that overexpression of CD27 activates NF-kappaB and stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK). Paper-1453876. Acute exposure of cerebellar granule neurons to ethanol suppresses stress-activated protein kinase-1 and concomitantly induces AP-1. Paper-8854496. Increase of RhoB in gamma-radiation- induced apoptosis is regulated by c-Jun N-terminal kinase in Jurkat T cells. Paper-14222218. Ionizing radiation stimulates a Grb2- mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase. Paper-319669. Androgen.AR induces expression of p21 that in turn inhibits tumor necrosis factor alpha- induced JNK and apoptosis. Paper-14157258. We show that JNK is rapidly activated by TGF-beta in a SMAD-independent manner and phosphorylates Smad3 outside its -SSXS motif. Paper-2057145. We concluded that RSV triggered autophagic cell death in CML cells via both JNK- mediated p62 overexpression and AMPK activation. Paper-14232612. The SH3 domain-containing adaptor HIP-55 mediates c-Jun N-terminal kinase activation in T cell receptor signaling. Paper-10042597. Further, p53 participates in a feedback mechanism with JNK to regulate this apoptotic process and is oppositely regulated by JNK1 and JNK2. Paper-10758369. Here, we report that androgen via p21 inhibits tumor necrosis factor alpha- induced JNK activation and apoptosis. Paper-14157258. Overexpression of PP2A catalytic subunit induced dephosphorylation of ASK1 pSer967 and activation of c-Jun N-terminal kinase (JNK). Paper-12769322. BMP4 inhibits proliferation and promotes myocyte differentiation of lung fibroblasts via Smad1 and JNK pathways. Paper-10760113. Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus. Paper-9429529. The results suggest that livin may exert anti-apoptotic action on SPC-A1 by activating JNK1 signaling pathway and inhibiting caspase-3 activation. Paper-14141792. Furthermore, ASK1-dependent phosphorylation was required for JSAP1 to recruit and thereby activate JNK in response to H(2)O(2). Paper-9173055. CONCLUSIONS: WWOX induces apoptosis and inhibits human HCC cell growth through a mechanism enhanced by JNK inhibition. Paper-12965544. Expression of a dominant negative mutant of JNK1 suppressed hypoxia- induced JNK1 activation as well as bFGF gene expression. Paper-2157708. PRINCIPAL FINDINGS: We report that in vivo, the activity of JIP1- JNK complexes is downregulated by VRK2 in response to interleukin-1beta. Paper-12749478. Constitutive activation of TAK1 by HTLV-1 tax-dependent overexpression of TAB2 induces activation of JNK- ATF2 but not IKK-NF-kappaB. Paper-13406987. DCA stimulated JNK activation and the JNK inhibitor SP600125 blocked DCA- induced DR5/ TRAIL-R2 mRNA and protein expression. Paper-10287042. Both binding and catalytic activation of MKP-1 are abrogated by mutation of a conserved docking site in ERK2, p38alpha, and JNK1 MAP kinases. Paper-8778653. Specific inhibitors of JNK kinase and ERK1/2 kinase were found to suppress the H. pylori- induced MMP-1 expression and activity. Paper-11350719. Autophagy and apoptosis are fundamental cellular pathways that are both regulated by JNK- mediated Bcl-2 phosphorylation. Paper-13003478. Inhibition of arachidonate 5-lipoxygenase triggers prostate cancer cell death through rapid activation of c-Jun N-terminal kinase. Paper-9818614. We also show that p53 up-regulates the MAP4K4 gene and activates the c-Jun NH2-terminal kinase ( JNK) pathway to drive apoptosis. Paper-10780190. Hsp72 and stress kinase c-jun N-terminal kinase regulate the bid-dependent pathway in tumor necrosis factor-induced apoptosis. Paper-9441147. Wnt-3a and Dickkopf-1 stimulate neurite outgrowth in Ewing tumor cells via a Frizzled3- and c-Jun N-terminal kinase-dependent mechanism. Paper-14292373. Conversely, specific siRNA against CCDC134 activates Elk1 transcriptional activity and promotes Erk and JNK/ SAPK phosphorylation. Paper-14332916. Recruitment of JNK to JIP1 and JNK-dependent JIP1 phosphorylation regulates JNK module dynamics and activation. Paper-9810405. Kinase assays showed that c-Jun N-terminal kinase (JNK) was also activated with activation kinetics corresponding to that of K8 phosphorylation. Paper-9159070. The transactivation domain of NFAT3 is found between amino acids (aa) 113 and 260 and includes the phosphorylation targets of JNK1 and JNK2. Paper-12496586. We have also identified an additional domain between MEKK1- and MEKK4- binding sites as being required for JNK activation by Axin. Paper-9989017. JNK- mediated phosphorylation of paxillin in adhesion assembly and tension-induced cell death by the adenovirus death factor E4orf4. Paper-14342980. Thus Filamin A is a novel member of the group of scaffold proteins whose function is to link two MAPKKs together and promote JNK activation. Paper-14686837. RNA interference-mediated inhibition of JNK1 strongly inhibited M-RIP mRNA expression induced by EGF, as well as the invasion of HeLa cells. Paper-12933642. Moreover, our findings support a role for JNK- mediated paxillin phosphorylation in adhesion growth and stabilization during tension signaling. Paper-14342980. Miz1 is a signal- and pathway-specific modulator or regulator (SMOR) that suppresses TNF-alpha- induced JNK1 activation. Paper-14073922. These results clearly indicate that CCDC134 is a novel member of the secretory family and down-regulates the Raf-1/MEK/ ERK and JNK/ SAPK pathways. Paper-14332916. When expressed in mammalian cells, MKP5 blocks the enzymatic activation of MAP kinases with the selectivity p38 approximately JNK/ SAPK >> ERK. Paper-2048174. We investigated the function of WWOX in human hepatocellular carcinoma ( HCC) and the effect of JNK inhibition on WWOX-mediated apoptosis. Paper-12965544. CRK adaptor protein expression is required for efficient replication of avian influenza A viruses and controls JNK-mediated apoptotic responses. Paper-15160018. IL-1 beta induces urokinase-plasminogen activator expression and cell migration through PKC alpha, JNK1/2, and NF-kappaB in A549 cells. Paper-13590703. Thus, JNK function might be modulated by targeting MKK-7 to suppress cytokine-mediated FLS activation while leaving other stress responses intact. Paper-12085129. Dual targeting of IGF-1R and PDGFR inhibits proliferation in high-grade gliomas cells and induces radiosensitivity in JNK-1 expressing cells. Paper-12604887. We suggest that VEGF induced by HBO is through c-Jun/ AP-1 activation, and through simultaneous activation of ERK and JNK pathways. Paper-11349116. Tumor necrosis factor-alpha down-regulates human Cu/ Zn superoxide dismutase 1 promoter via JNK/ AP-1 signaling pathway. Paper-12169501. RESULTS: We found that inducible expression of RbAp46 activated the c-Jun N-terminal kinase (JNK) signaling pathway and triggered apoptosis in Saos-2 cells. Paper-10115321. NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/ JNK cascade via a conserved regulatory domain. Paper-989267. Our results reveal that H2O2-induced MST3- mediated cell death involves suppressing both a JNK survival pathway and up-regulation of HO-1. Paper-13992823. Utilizing an estrogen ligand-activated MEKK3 derivative, we furthermore demonstrate that MEKK3 regulates the SAPK and the ERK pathway directly. Paper-900260. Additionally, GNRH-induced Egr1 gene expression is mediated by MAPK8/9 and MAPK1/3, and both are critical for Lhb gene transcription. Paper-14145635. JNK- mediated turnover and stabilization of the transcription factor p45/ NF-E2 during differentiation of murine erythroleukemia cells. Paper-14209165. NFAT3 transactivation activity was suppressed in JNK1(-/-) or JNK2(-/-) mouse embryonic fibroblast (MEF) cells compared with wild-type MEF cells. Paper-12496586. NIK likely functions upstream of MEKK1 to activate this pathway; a dominant-negative MEK kinase 1 ( MEKK1) blocks activation of SAPK by NIK. Paper-989267. Expression of a series of wild-type and dominant-negative kinases indicated an ASK1/Jun N-terminal protein kinase 1 ( JNK1) pathway phosphorylated BCL-2 in vivo. Paper-2050254. The ability of MEKK3 to simultaneously activate the SAPK and ERK pathways is remarkable, given that they have divergent roles in cellular homeostasis. Paper-900260. The data demonstrate that Pax2 is a new target for the JNK signaling module and point to a novel mechanism for mediating Pax-dependent transcription regulation. Paper-9154193. Activation of JNK by either upstream kinase MEKK1 or DLK or by expression of Wnt signaling proteins significantly enhances Pax2 phosphorylation in cells. Paper-9154193. Regulation of IGFBP6 gene and protein is mediated by the inverse expression and function of c-jun N-terminal kinase (JNK) and NFkappaB in a model of oral tumor cells. Paper-14337563. The TNF-alpha- induced PTX3 expression was blocked by SP600125, a JNK-specific inhibitor, but not by the inhibitors against NF-kappaB, ERKs, or p38 MAPK. Paper-11281687. The upregulation of Beclin 1 expression could be blocked by SP600125 (a specific inhibitor of JNK) or a small interfering RNA (siRNA) directed against JNK1/2 or c-Jun. Paper-13524626. These data suggest that polyozellin suppresses iNOS expression by inhibiting the activation of NF-kappaB and SAPK/JNK, leading to the inhibition of NO production. Paper-12153337. Here, we showed that the nuclear factor of activated T3 ( NFAT3) is phosphorylated by JNK1 or JNK2 at Ser(213) and Ser(217), which are located in the conserved SP motif. Paper-12496586. Our results suggest that Stat3 is a target of JNK that may regulate Stat3 activity via both Ser-727 phosphorylation-dependent and -independent mechanisms. Paper-8299703. Adaptor proteins CRK and CRKL associate with the serine/ threonine protein kinase GCKR promoting GCKR and SAPK activation. Paper-2103162. Here, we report that the nuclear components Daxx and Ras-association domain family 1C (RASSF1C) link DNA damage to SAPK/ JNK activation in HeLa cells. Paper-12073843. MKP1 regulates the induction of MUC5AC mucin by Streptococcus pneumoniae pneumolysin by inhibiting the PAK4- JNK signaling pathway. Paper-13067198. Taken together, these findings establish a major role for DAPk and its specific interaction with PKD in regulating the JNK signaling network under oxidative stress. Paper-12576070. Full-length MKK7 containing combined D1/D2 mutations was compromised for binding to JNK1 and exhibited reduced JNK1 kinase activity when compared with wild-type MKK7. Paper-11845266. JNK-specific inhibitor SP600125 induces growth inhibition via induction of G1 or G2/M arrest in U266 and MM.1S multiple myeloma cell lines, respectively. Paper-10040716. Pharmacological blockade of MAPK activities suggested that pro- MMP-7 expression was induced via JNK1/2 activation, but not in the case of ERK1/2 or p38 MAPK. Paper-11011812. We used microarray techniques to compare the gene expression profiles of epidermal growth factor (EGF)- stimulated HeLa cells with and without JNK1 siRNA treatment. Paper-12933642. Resveratrol promotes autophagic cell death in chronic myelogenous leukemia cells via JNK- mediated p62/ SQSTM1 expression and AMPK activation. Paper-14232612. Together, our results suggest that Gemin5 functions as a scaffold protein for the ASK1- JNK1 signaling module and thereby potentiates ASK1-mediated signaling events. Paper-13341457. CONCLUSION: JNK1 stimulated and mediated the effects of IFN and TNF-alpha on XAF1 expression through transcriptional regulation by induction of IRF-1. Paper-13522880. We found that HDRP associates with c-Jun N-terminal kinase (JNK) and inhibits its activity, thus explaining the inhibition of c-Jun phosphorylation by HDRP. Paper-11825889. An XAF1 promoter reporter pLUC107 with WT or mutated interferon regulatory factor 1- binding element (IRF-E) was used to assess JNK1-induced transcription by dual luciferase assay. Paper-13522880. Here we show that the PAK4- JNK signaling pathway acted as a negative regulator for Streptococcus pneumoniae pneumolysin- induced MUC5AC mucin transcription. Paper-13067198. DNA-PKcs induces T-cell death by activating the JNK pathway and upregulating the apoptogenic BH3-only proteins Bim and Bmf. Paper-15426106. Downregulation of cyclin D1- CDK4 protein in human embryonic lung fibroblasts (HELF) induced by silica is mediated through the ERK and JNK pathway. Paper-13040688. The activated JNK could directly phosphorylate R-Smads in vitro at the same sites that were phosphorylated in response to TGF-beta or HGF in vivo. Paper-10646972. Overexpressed PS1 suppressed the stress- induced stimulation of stress-activated protein kinase (SAPK)/c-Jun NH(2)-terminal kinase (JNK) in human embryonic kidney 293 cells. Paper-8787641. ETBR- stimulated ppET-1 promoter activity was partially diminished by the expression of dominant negative forms of c-Jun N-terminal kinase (JNK1APF) or MAPK/ERK kinase (MEKK97M). Paper-9280459. JNK1 differentially regulates osteopontin- induced nuclear factor- inducing kinase/ MEKK1-dependent activating protein-1-mediated promatrix metalloproteinase-9 activation. Paper-12466851. HPK1 specifically activates the SAPK/ JNK pathway after transfection into COS1 cells, but does not stimulate the p38/RK or mitogen-activated ERK signaling pathways. Paper-855604. c-Jun N-terminal kinase ( JNK1) upregulates XIAP-associated factor 1 ( XAF1) through interferon regulatory factor 1 ( IRF-1) in gastrointestinal cancer. Paper-13522880. Studies of MAPK (mitogenactivated protein kinase) interactions demonstrated that SPAG9 interacted with higher binding affinity to JNK3 and JNK2 compared with JNK1. Paper-11183674. Here, we reported that TOPK regulates UVB- induced c-Jun-NH2-kinase 1 ( JNK1) activity, and is essential for H-Ras-induced activator protein-1 activity and cell transformation. Paper-13263824. Intracellular JNK, p38 MAPK and NF-kappaB regulate IL-25 induced release of cytokines and chemokines from costimulated T helper lymphocytes. Paper-12557038. Taken together, these findings showed that TOPK positively modulated UVB- induced JNK1 activity and played a pivotal role in JNK1-mediated cell transformation induced by H-Ras. Paper-13263824. Tumor necrosis factor alpha-induced interleukin-32 is positively regulated via the Syk/protein kinase Cdelta/ JNK pathway in rheumatoid synovial fibroblasts. Paper-13652299. TGF-beta1 stimulates human AT1 receptor expression in lung fibroblasts by cross talk between the Smad, p38 MAPK, JNK, and PI3K signaling pathways. Paper-13411972. Tumor necrosis factor-alpha-elicited stimulation of gamma-secretase is mediated by c-Jun N-terminal kinase-dependent phosphorylation of presenilin and nicastrin. Paper-13013741. Mechanical stretch decreases FAK phosphorylation and reduces cell migration through loss of JIP3- induced JNK phosphorylation in airway epithelial cells. Paper-13940914. In addition, pretreatment of cells with NF-kappaB inhibitor ( MG-132) or JNK inhibitor (SP600125) significantly inhibited ICAM-1 expression promoted by HDM extract. Paper-12592724. The PEA-15- induced JNK activation depends on the phosphorylation of PEA-15 at both phosphorylation sites ( serine 104 and serine 116). Paper-15203271. Here, we show that the mitogen-activated protein kinase kinase kinase 1 (MEKK1)/c-Jun-NH(2)-kinase ( JNK) pathway represses hTR expression by a mechanism that involves Sp1 and Sp3. Paper-10825893. SDF-1alpha enhanced NMDA activity indirectly via Src phosphorylation, whereas gp120(IIIB) probably activated the NMDA receptor directly and phosphorylated JNK. Paper-14706257. We found that CCR7 induced a G(i)-dependent activation of MAPK members ERK1/2, JNK, and p38, with ERK1/2 and p38 controlling JNK. Paper-10734828. Glial cell-derived neurotrophic factor ( GDNF) promotes low-grade Hs683 glioma cell migration through JNK, ERK-1/2 and p38 MAPK signaling pathways. Paper-12207591. Overall the results suggest that Vpr-(52-96)-activated JNK plays a key role in inducing apoptosis through the down-regulation of antiapoptotic Bcl2 and c-IAP1 genes. Paper-13105229. These data indicate that the AP-1-like binding site in the MFNLP sequence gives rise to a higher inducibility of natural HIV-LTRs by the SAPK/ JNK signaling pathway. Paper-8360424. We also provide evidence during rolling and adhesion of platelets to vWF that platelet GPIb- vWF interaction triggers alphaIIbbeta3 activation in a JNK1-dependent manner. Paper-12534150. Interference with Ubc13 function or expression inhibits both TNF- and TRAF2- mediated GCKR and SAPK activation, but has a minimal effect on ASK1 activation. Paper-9732252. The inhibition of JNK activation or the suppression of c-Jun or JunD expression with siRNA impaired the effects of adrenomedullin on cell proliferation and on cyclin D1. Paper-13616281. Initial experiments showed that an inhibitor of c-Jun N-terminal kinase (JNK) downregulated basal CYP27A1 promoter activity whereas overexpression of JNK slightly enhanced promoter activity. Paper-15645525. Silencing JNK expression with siRNA reversed the phosphorylation of c-Jun induced by adrenomedullin, indicating that JNK is responsible of c-Jun activation. Paper-13616281. Our results indicate that perturbation of tensional homeostasis by E4orf4 involves JNK- regulated changes in paxillin adhesion dynamics that are required to engage the death pathway. Paper-14342980. Pax2 can form a complex with the JNK scaffolding protein JIP1, and this interaction is enhanced by activation of the JNK signaling module with the upstream kinase DLK. Paper-9154193. Moreover, JNK phosphorylates Cdh1 directly, during G2 and early mitosis, changing its subcellular localization and attenuating its ability to activate the APC/C during G2/M. Paper-15276637. Previous data established that in human bronchial epithelial (HBE1) cells, both genes for glutamate cysteine ligase ( GCL) are induced by HNE through the c-Jun N-terminal kinase (JNK) pathway. Paper-12762774. Here, we demonstrate that TNF-alpha triggers JNK-dependent serine/ threonine phosphorylation of PS1 and NCT to stimulate gamma-secretase activity. Paper-13013741. These findings suggest that the metabolites of arachidonate 5-lipoxygenase promote survival of prostate cancer cells involving down-regulation of stress-activated protein kinase. Paper-9818614. c-Jun N-terminal kinase (JNK)- mediated cell signaling pathways are regulated endogenously in part by protein-protein interactions with glutathione S-transferase P1-1 ( GSTP1-1) (). Paper-8986561. In this study, we found that stress-activated protein kinase (SAPK)1/ c-Jun N-terminal kinase 1 and SAPK2/p38 are involved in the control of MCP-1-induced MonoMac6 cell migration. Paper-10371976. Finally, we used Filamin-A-deficient cells to show that Filamin A enhances MKK7 activation and is important for synergistic stress- induced JNK activation in vivo. Paper-14686837. RESULTS: IL-1beta- induced JNK phosphorylation was dependent on MKK-7 but not on MKK-4; however, anisomycin-activated JNK required both kinases. Paper-12085129. IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase ( JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Paper-10202453. Overexpression of JKAP in human embryonic kidney 293T cells specifically activated c-Jun N-terminal kinase (JNK) but not p38 and extracellular signal-regulated kinase 2. Paper-9171289. In conclusion we found that IGF-1R and PDGFR co-inhibition caused an increased cell death in two HGG cell line and induced the radiosensitization of the JNK1 expressing cell line. Paper-12604887. Conditional expression of the mitogen-activated protein kinase ( MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells. Paper-1079902. Interestingly, TAM67, a dn form of c-Jun, did not mediate the JNK-dependent effect on TNF-dependent apoptosis, indicating that other molecular targets are essential to confer this mechanism. Paper-9520662. In contrast, human SIRT1 was phosphorylated by JNK1 on three sites: Ser27, Ser47, and Thr530 and this phosphorylation of SIRT1 increased its nuclear localization and enzymatic activity. Paper-14619807. Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 ( MKK6); comparison of its substrate specificity with that of other SAP kinases. Paper-1091705. In our present study, we have shown that another MEKK family member, MEKK4, also binds to Axin in vivo and mediates Axin- induced JNK activation. Paper-9989017. Distinct role of c-Jun N-terminal kinase isoforms in human neutrophil apoptosis regulated by tumor necrosis factor-alpha and granulocyte-macrophage colony-stimulating factor. Paper-14311928. The bFGF- mediated surface cadherin downregulation was significantly reversed only when the HUVECs were treated with JNK inhibitor (SP600125), but not ERK (PD98059) or p38 inhibitor (SB203580). Paper-12705049. Treatment with the JNK inhibitor SP600125 and silencing of both JNK1 and JNK2 with siRNA inhibited UFP- stimulated O(2)(-) production and mRNA expression of HO-1 and TF. Paper-13634614. VRK2 binding to the JIP1 signalosome prevents the association of JNK and results in a reduction in its phosphorylation and downregulation of AP1-dependent transcription. Paper-12749478. Study of inhibitors of Hsp70 induction or pre-induction of Hsp70 indicated that induced Hsp70 was involved in the suppression of JNK activation thereby inhibiting apoptotic cell death. Paper-10015936. JNK- ATF-2 inhibits thrombomodulin ( TM) expression by recruiting histone deacetylase4 ( HDAC4) and forming a transcriptional repression complex in the TM promoter. Paper-14648125. NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/ stress-activated protein kinase signaling pathway. Paper-1812264. We previously reported that a small peptide based on amino acids 143-153 of the c-Jun N-terminal kinase (JNK)- binding domain of JIP-1 functioned as an in vitro inhibitor of JNK activity. Paper-10524390. Overexpression of BRCA1 was shown to induce an apoptotic signaling pathway involving the c-Jun N-terminal kinase ( JNK), but the signaling steps upstream and downstream of JNK were not delineated. Paper-8600123. These findings suggest that ERK2- mediated induction of MKP-1 may play an important role in preferentially attenuating signaling through the p38 MAPK and SAPK signal transduction pathways. Paper-1079902. Furthermore, CrkII recruits JNK1 to a p130Cas multiprotein complex where it may be activated through a hematopoietic progenitor kinase 1- and mitogen-activated protein kinase kinase 4-dependent pathway. Paper-9008573. A POSH mutant that is unable to bind Akt2 (POSH W489A) exhibits enhanced- binding to MLK3, and this increase in binding is accompanied by increased activation of the JNK signaling pathway. Paper-10041354. Forced expression of a constitutively active form of RhoA increased JNK phosphorylation and overcame the inhibitory effect of atorvastatin on MMP2 activity and cell invasion. Paper-13067161. Thalidomide inhibited EGF- induced phosphorylation of extracellular signal regulated kinase (ERK) 1/2, but not p38 and stress-activated protein kinase (SAPK)/JNK. Paper-12916800. CRTAM expression was reduced in activated CD8(+) T cells treated with the JNK inhibitor SP600125, indicating that CRTAM expression is driven by the JNK-AP-1 signaling pathway. Paper-14029346. Insulin-stimulated Ser(307) phosphorylation was reduced 80% in cells lacking JNK1 and JNK2 or in cells expressing a mutant Irs1 protein lacking the JNK binding site. Paper-9840745. Furthermore, JNK2 and JNK3 also associate with p53 in vivo, indicating that not only JNK1, but also JNK2 and JNK3 are p53 N-terminal serine 34 kinases. Paper-1245211. Together, our results suggest an important role for cross talk among Smad, p38 MAPK, JNK, and PI3K pathways in mediating the augmented expression of hAT(1)R following TGF-beta1 treatment in hPFB. Paper-13411972. We further demonstrate that the Stress-Activated-Protein-Kinase ( SAPK) target sites of ATF2, Thr69 and Thr71 are not required for the formation of the p300/ CBP- ATF2 multiprotein complex. Paper-1848512. Furthermore, the PR8-SH3-mf-1 virus was unable to phosphorylate apoptosis signal-regulating kinase 1 ( ASK1) but induced higher levels of c-jun N-terminal kinase (JNK) phosphorylation than the WT virus. Paper-15107486. Activation of SAPK through the chimeric molecules always correlated with their ability to activate NF-kappaB activity and to rescue the cells from apoptosis induced by antigen receptor ligation. Paper-1652185. Our data suggest that melittin can synergize with TRAIL in the induction of HCC cell apoptosis by activating the TAK1- JNK/ p38 pathway but inhibiting the IkappaBalpha kinase-NFkappaB pathway. Paper-13597083. Forced expression of WWOX in SNU387 cells decreased FGF2- mediated proliferation and enhanced apoptosis induced by staurosporine and the JNK inhibitor SP600129. Paper-12965544. However, TGF-beta1- induced FXII expression was repressed only by the JNK inhibitor and JNK and Smad3 antisense oligonucleotides but not by MEK, p38, or phosphoinositide 3-kinase blockers. Paper-14695417. Here, we report that TNF activates GCKR and the SAPK pathway in a manner that depends upon TRAF2 and Ubc13, a member along with Uev1A of a dimeric ubiquitin-conjugating enzyme complex. Paper-9732252. Furthermore, a mutant form MKP-7 functioned as a dominant negative particularly against the dephosphorylation of JNK, suggesting that MKP-7 works as a JNK-specific phosphatase in vivo. Paper-9047286. MKP-5 binds to p38 and SAPK/JNK, but not to MAPK/ ERK, and inactivates p38 and SAPK/JNK, but not MAPK/ ERK. p38 is a preferred substrate. Paper-1926448. We studied the role of c-Jun N-terminal kinase (JNK) in human neutrophils stimulated by tumor necrosis factor-alpha ( TNF-alpha) and granulocyte-macrophage colony-stimulating factor ( GM-CSF). Paper-14311928. Here we have demonstrated that mechanical strain-dependent induction of the CCN1 gene involves signaling cascades through RhoA- mediated actin remodeling and the p38 stress-activated protein kinase ( SAPK). Paper-13933709. Oligomerization of the TRAF2 effector domain results in specific binding to MEKK1, a protein kinase capable of JNK, p38, and IKK activation, and induction of TNF-alpha and IL-1 responsive genes. Paper-1875239. Here we demonstrated that MKK7 recognizes its target JNK by a novel mechanism involving a partially cooperative interaction of three low affinity D-sites in the N-terminal domain of MKK7. Paper-11845266. The present study demonstrated that AM is expressed in ovarian epithelial carcinoma tissue and bFGF can induce the expression of AM through the JNK- AP-1 pathway in ovarian epithelial carcinoma cell line CAOV(3). Paper-13935478. These studies indicate that the MLK3/ JNK1 axis mediates G17-induced gastric cancer cell migration, which can be targeted for designing novel therapeutic strategies for treating gastric malignancies. Paper-14179543. Forced Gadd45beta expression in human FLS attenuated tumor necrosis factor- induced signaling through the JNK pathway, reduced the activation of activator protein 1, and decreased the expression of MMP genes. Paper-14092777. JNK1 stimulated interferon regulatory factor 1 ( IRF-1) expression, whereas both IRF-1 small-interfering RNA and site mutation of IRF-E within XAF1 promoter abrogated the effect of JNK1. Paper-13522880. Conditional expression of MAP kinase phosphatase-2 protects against genotoxic stress- induced apoptosis by binding and selective dephosphorylation of nuclear activated c-jun N-terminal kinase. Paper-10995986. Differential regulation of CD44 expression by lipopolysaccharide (LPS) and TNF-alpha in human monocytic cells: distinct involvement of c-Jun N-terminal kinase in LPS- induced CD44 expression. Paper-9262123. Polymeric immunoglobulin receptor- mediated invasion of Streptococcus pneumoniae into host cells requires a coordinate signaling of SRC family of protein-tyrosine kinases, ERK, and c-Jun N-terminal kinase. Paper-15498115. PD-098059, specific inhibitor of p42/ p44 MAPK pathway, counteracts the apoptotic effect of IL-1beta, whereas SB-203580, specific inhibitor of p38 stress- activated protein kinase ( SAPK) pathway, is ineffective. Paper-8613029. Gemin5 physically interacted with ASK1 as well as with the downstream kinases SEK1 and c-Jun NH(2)-terminal kinase ( JNK1), and it potentiated the H(2)O(2)-induced activation of each of these kinases in intact cells. Paper-13341457. Further, it is demonstrated that GH induced ERK1/2 cascade regulates production of TNF-alpha and IL-1beta in macrophages, whereas JNK cascade mediated the production of TNF-alpha, IFN-gamma and IL-12. Paper-13076675. In addition, transfection of siRNA against phosphoinositide 3-kinase ( PI3K) p110beta attenuated LPS- induced IL-12 production and JNK1 phosphorylation, while not affecting JNK2 phosphorylation. Paper-15212050. JNK activation is regulated by phosphorylation of specific tyrosine and threonine residues sequentially catalysed by MKK4 and MKK7, which are both dual-specificity MAPKKs (MAPK kinases). Paper-14686837. However, JNK1 did not phosphorylate c-Rel, NF-kappaB, and IkappaB alpha in vitro, indicating that c-Rel may serve as a docking molecule to allow JNK1 phosphorylation of certain Rel-associated proteins. Paper-538549. Specific inhibitors of SAPK/JNK significantly reduced AECA- induced chemokine production and phosphorylation of c-Jun and activating transcription factor-2 and abrogated protein expression of MICA but not VAP-1. Paper-13409199. We further demonstrate that JNK1, activated by its upstream kinase MKK7, negatively regulated the tyrosine phosphorylation and DNA binding and transcriptional activities of Stat3 stimulated by EGF. Paper-8299703. Functional investigation reveals that overexpression of CCDC134 and its purified protein significantly inhibit transcriptional activity of Elk1 and phosphorylation of Erk and JNK/ SAPK but not p38 MAPK. Paper-14332916. Stress-activated protein kinase ( SAPK) was not activated by the cytokines alone, whereas adding the cytokine TNF-alpha to NH2- stimulated cells resulted in activation of SAPK after 15 min. Paper-8917324. Tumor necrosis factor (TNF)- induced activation of the c-jun N-terminal kinase ( JNK, also known as SAPK; stress-activated protein kinase) requires TNF receptor-associated factor 2 ( TRAF2). Paper-1597944. The present study corroborated this hypothesis by demonstrating that JNK binding to JIP1 is necessary for stimulus-induced dissociation of DLK from JIP1, for DLK oligomerization, and for JNK activation. Paper-9810405. The major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase ( JNK), p38 and extracelluar signal- regulated kinase ( ERK) are three kinases that have been shown to regulate apoptosis. Paper-12774694. Actin-binding protein-280 binds the stress-activated protein kinase ( SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells. Paper-900256. The inability of MKP-2 to dephosphorylate ERK in vivo is also not due to the inability of Flag- MKP-2 to bind both ERK and JNK; phosphorylated forms of each kinase are co-precipitated with both WT and CI- MKP-2. Paper-10995986. Here we have identified human Rev7 (hRev7)/MAD2B/ MAD2L2 as an interaction partner for Elk-1 and demonstrate that hRev7 acts to promote Elk-1 phosphorylation by the c-Jun N-terminal protein kinase ( JNK) MAP kinases. Paper-12480011. Moreover, blockade of the MAPK cascade by the aminomethoxyflavone MEK1 inhibitor PD-98059 unexpectedly activated p46- JNK1/p54- JNK2 and induced apoptosis in a manner qualitatively resembling that of sphingosine. Paper-1282791. JNK inhibition had no effect on TGF-beta1- induced Smad3 phosphorylation, association with Smad4, and its translocation into the nucleus but strongly suppressed Smad3-DNA complex formation. Paper-14695417. We further show that DAPk activates PKD in cells and that induction of JNK phosphorylation by ectopically expressed DAPk can be attenuated by knocking down PKD expression or by inhibiting its catalytic activity. Paper-12576070. TNF-alpha stimulates the JNK, ERK, and p38 mitogen- activated protein kinases and the NF-kappaB pathway by recruiting RIP1 and TRAF2 to the TNF receptor 1. Paper-10839715. Hence, ASK1 is a common mediator of TRAF- regulated SAPK and apoptosis signaling, and the TRAF2 - ASK1 connection completes the signaling cascade from TNF to SAPK/ JNK activation. Paper-8307443. Both Hsp72 and Delta Hsp72EEVD blocked activation of the stress kinase c-jun N-terminal kinase (JNK) by TNF, and specific inhibition of JNK similarly temporarily blocked Bid activation and the downstream apoptotic events. Paper-9441147. Suppression of p38 MAPK and JNK via Akt- mediated inhibition of apoptosis signal-regulating kinase 1 constitutes a core component of the beta-cell pro-survival effects of glucose-dependent insulinotropic polypeptide. Paper-14067494. In signaling context, the interaction of c-FLIP(L) with Daxx is likely to inhibit JNK activation by preventing the normal interaction of Daxx and Fas, which is known to lead to apoptosis via JNK activation. Paper-10084034. Apoptosis signal-regulating kinase (ASK) 1 is a MAP kinase kinase kinase that activates the JNK and p38 mitogen-activated protein (MAP) kinase cascades in response to environmental stresses such as reactive oxygen species. Paper-9173055. However, when coexpressed, they formed a strong complex with GCKR, thereby providing a potential mechanism for TRAF and TANK synergy in GCKR- mediated SAPK activation, which is important in TNF family receptor signaling. Paper-2078821. Chromatin immunoprecipitation showed that levels of immunoreactive Sp1 associated with the hTR promoter were low in comparison with Sp3 in control cells but increased after JNK inhibition with a reciprocal decrease in Sp3 levels. Paper-10825893. SEK-1(KR) completely inhibited ET-1- induced SAPK activation without affecting activation of the other MAP kinases implicated in the hypertrophic response, p38 and extracellular signal-regulated protein kinases (ERK)-1/ERK-2. Paper-1610371. This is evidenced by the ability of CrkII, in a PI 3-kinase-independent manner, to diminish the activation of p44/42 mitogen-activated protein kinase in response to both hGH and hIGF-1 and to inhibit the activation of SAPK by hIGF-1. Paper-8387073. IFN-alpha induced the expression of IFIT4 and STAT1 in THP-1 cells, and this process was significantly antagonized by the specific inhibitors of both PKCdelta and JNK or their dominant negative mutants respectively. Paper-14331818. These results suggest that a cross-talk mechanism exists between the MAPK and SAPK signal transduction pathways in U937 cells and that PMA- mediated SAPK activation may involve the MAPK pathway. Paper-477823. In vitro kinase assay demonstrated that IL-1beta-or TNFalpha induced JNK activity was only MKK-7 dependent, while anisomycin-activated JNK was both MKK-4 and MKK-7 dependent. Paper-12085129. JNK regulates SMAD- and TGF-beta-mediated transcriptional responses, yet JNK activators only partially stimulate transcriptional responses characteristic of TGF-beta without coincident SMAD pathway activation. Paper-2057145. Expression of catalytically inactive JNK1 blocks NAIP and ML-IAP protection against ICE- and TNF-alpha-induced apoptosis, indicating that JNK1 activation is necessary for the antiapoptotic effect of these proteins. Paper-9195765. This report documents the fact that inhibition of arachidonate 5-lipoxygenase induces rapid activation of c-Jun N-terminal kinase (JNK) in human prostate cancer cells which is prevented by the 5-lipoxygenase metabolite, 5(S)-HETE. Paper-9818614. We conclude that specific strategies to modulate persistent activation of the JNK pathway may be beneficial in preventing disease progression and treating myeloma- associated bone disease by inhibiting DKK1 expression. Paper-13214135. JNK pathway involved HGF and TGF-beta- mediated infiltration potency since a JNK inhibitor SP600125 caused the reduction of invasive capacity induced by HGF and TGF-beta signals. Paper-10646972. This work describes a novel mode of regulation of MLK3, by which JNK- mediated feedback phosphorylation of MLK3 regulates its activation and deactivation states by cycling between Triton-soluble and Triton-insoluble forms. Paper-12060573. Transactivation of naturally occurring HIV-1 long terminal repeats by the JNK signaling pathway. The most frequent naturally occurring length polymorphism sequence introduces a novel binding site for AP-1 factors. Paper-8360424. Adrenomedullin promotes cell cycle transit and up-regulates cyclin D1 protein level in human glioblastoma cells through the activation of c-Jun/ JNK/ AP-1 signal transduction pathway. Paper-13616281. RNAi-mediated depletion of ILK induced activation of JNK and its target, c-Jun, resulting in growth of ERMS cells, whereas in ARMS cells, it led to loss of JNK/c-Jun signaling and suppression of growth both in vitro and in vivo. Paper-13815125. The upregulation of costimulation-induced IL-25 receptors and release of cytokines and chemokines from IL-25 treated costimulated Th cells were differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Paper-12557038. A JNK inhibitor antagonized the negative effects of TNF-alpha on SOD1 promoter activity, suggesting that JNK signaling through c-Jun protein activation is critical for the TNF-alpha-dependent SOD1 repression. Paper-12169501. This study was carried out to evaluate whether low Gadd45beta expression in RA enhances JNK activation and overproduction of MMPs in RA, and whether Gadd45beta deficiency increases arthritis severity in passive K/BxN murine arthritis. Paper-14092777. Here, we report that the transcription factor Myc-interacting zinc-finger protein 1 ( Miz1) selectively suppresses TNF-alpha- induced JNK1 activation and cell death independently of its transcription activity. Paper-14073922. We then examined the involvement of mitogen-activated protein kinases (MAPKs) including c-Jun N-terminal protein kinase ( JNK), extracellular signal-regulated kinases (ERKs) and p38 MAPK in Hs683 cell migration induced by GDNF. Paper-12207591. Overexpression of the protein kinases mixed-lineage kinase-2 ( MLK2) or mitogen-activated protein kinase (MAPK) kinase kinase-1 (MEKK1) is known to trigger the activation of stress-activated protein kinase (SAPK1)/c-Jun N-terminal kinase (JNK). Paper-1500895. Our results indicate that both MKK6 to p38 and MKK7 to SAPK/JNK signaling pathways are activated in a cyclosporin A-sensitive manner and contribute to IL-2 gene expression in T lymphocytes. Paper-1439812. Thus, our results show that in addition to being a transcription factor Miz1 acts as a signal- and pathway-specific modulator or regulator that specifically regulates TNF-alpha- induced JNK1 activation and cell death. Paper-14073922. Thus TNF-alpha causes a net up-regulation of MUC2 gene expression in cultured colon cancer cells because NF-kappaB transcriptional activation of this gene is able to counter-balance the suppressive effects of the JNK pathway. Paper-10736785. Here we demonstrate that overexpression of TRPM7 increased levels of cellular reactive oxygen species (ROS) and nitric oxide, causing the activation of p38 mitogen- activated protein kinase ( MAPK) and c-Jun N-terminal kinase (JNK). Paper-14644928. Direct activation of the stress-activated protein kinase ( SAPK) and extracellular signal- regulated protein kinase ( ERK) pathways by an inducible mitogen-activated protein Kinase/ ERK kinase kinase 3 (MEKK) derivative. Paper-900260. This study was designed to investigate the effect of c-Jun N-terminal kinase (JNK) 1 and 2 on TGF-beta(1)- regulated CTGF gene expression and corneal scar formation in telomerase-immortalized human corneal stroma fibroblast (THSF) cells. Paper-13881971. In conclusion, we present novel evidence that JNK regulates the expression of HIPK3 in prostate cancer cells, and this contributes to increased resistance to Fas receptor-mediated apoptosis by reducing the interaction between FADD and caspase-8. Paper-10249300. In summary, we have shown that ceramide potently activates the SAPK cascade but not the ERK cascade in endothelial cells, which contrasts to mesangial cells where ceramide activates the ERK pathway and has only a minor effect on the SAPK cascade. Paper-10273568. The TNF-alpha- induced activation of JNK1 is augmented in Miz1-deficient mouse embryonic fibroblasts ( Miz1(-/-) MEFs), but the augmentation is abrogated by reintroduction of Miz1 or its transcription-deficient mutant. Paper-14073922. In this report, we show that protein 4.1B/differentially expressed in adenocarcinoma of the lung-1 ( DAL-1) expression in meningioma cells in vitro results in JNK activation, which requires the sequential activation of Src, Rac1, and JNK. Paper-12009583. Its encoded protein is 366 amino acids long (calculated Mr 42 209), has a TGY dual phosphorylation motif in protein kinase subdomain VIII and displays highest overall similarity to the mammalian p38 stress activated protein kinase ( SAPK2), one subfamily of MAPKs. Paper-8475178. SAPK/JNK-specific inhibitor SP600125 slightly suppressed IL-6 production although no evident effects were obtained for TNF-alpha and IL-1beta; ERK1/2 inhibitor PD98059 blocked both TNF-alpha and IL-1beta, but not IL-6 production. Paper-12744605. Importantly, we discovered that GIP suppressed p38 MAPK and JNK via Akt- mediated changes in the phosphorylation state of the apoptosis signal-regulating kinase 1 in INS-1 cells and human islets, resulting in inhibition of its activity. Paper-14067494. GCKR (also referred to as KHS1) is a serine/ threonine protein kinase that has an STE20-like protein kinase domain and that stimulates the stress-activated protein kinase ( SAPK, also referred to as Jun kinase or JNK) pathway. Paper-2103162. Tumor necrosis factor (TNF)- induced germinal center kinase-related ( GCKR) and stress-activated protein kinase ( SAPK) activation depends upon the E2/E3 complex Ubc13-Uev1A/ TNF receptor-associated factor 2 ( TRAF2). Paper-9732252. Furthermore, JNK1 associated with c-Rel in vivo in Jurkat T cells by coimmunoprecipitation assays and bound directly to c-Rel in a yeast two-hybrid assay. c-Rel also competed with c-Jun in in vitro kinase assays. Paper-538549. Here, we demonstrate that Ad- ST13 ( ST13 mediated by adenovirus) activates apoptosis signal- regulated kinase ( ASK1) and c-Jun N-terminal kinase (JNK) but not p38 (mitogen-activated protein kinase) in human colorectal HCT116 cells. Paper-15135577. Our results demonstrated that JNK and Erks were required in B[a]PDE- induced cyclin D1 expression because the inhibition of JNK or Erks by a selective chemical inhibitor or dominant negative mutant robustly impaired the cyclin D1 induction by B[a]PDE. Paper-14094116. More importantly, we show here that the N-CoR- HDAC3 complex inhibits JNK activation through the associated GPS2 subunit and thus could potentially provide an alternative mechanism for hormone-mediated antagonism of AP-1 function. Paper-9202254. MEKK1 induced both stress-activated protein kinase ( SAPK) and extracellular signal-regulated protein kinase (ERK) activity; however, while the SAPK cascade stimulated ANF expression, activation of the ERK cascade inhibited expression. Paper-1038387. Knockdown of endogenous JNK1 expression via small interference RNA (JNK1-siRNA) inhibited G17-induced phosphorylation of c-Jun and migration, and overexpression of wild-type JNK1 or constitutive active JNK1 promoted G17-induced migration. Paper-14179543. The orphan receptor TR3 functions in the nucleus as a transcription factor to negatively or positively regulate gene expression. c-Jun N-terminal kinase (JNK) phosphorylation plays an important role in modulating the nuclear functions of TR3. Paper-12379283. Because interleukin-6 ( IL-6) is a growth factor for MM cells and inhibits apoptosis induced by dexamethasone and serum starvation, we examined whether IL-6 affects anti-Fas MoAb- induced apoptosis and activation of SAPK or p38 MAPK in MM cells. Paper-828338. In addition, the mitogen-activated protein family kinases, including c-Jun N-terminal kinase ( JNK) and extracellular signal- regulated protein kinase ( ERK) kinases, and the transcription factor c-Jun were all activated by phosphorylation after 6 h exposure to THDA. Paper-12842779. Previous studies from our laboratory have shown that protein 4.1B growth suppression in meningioma is associated with the activation of the c-Jun-NH(2)-kinase ( JNK) pathway and requires localization of a small unique region (U2 domain) of protein 4.1B to the plasma membrane. Paper-12009583. Exogenous PlGF induced specific activation of the stress-activated protein kinase ( SAPK) pathways, c-Jun-N terminal kinase (JNK) and p38 kinase, in primary term trophoblast with little to no induction of the extracellular signal regulated kinase (ERK-1 and -2) pathways. Paper-1804302. Sustained activation of p38 mitogen- activated protein kinase and c-Jun N-terminal kinase pathways by hepatitis B virus X protein mediates apoptosis via induction of Fas/ FasL and tumor necrosis factor ( TNF) receptor 1/ TNF-alpha expression. Paper-10649682. PlGF activation of flt-1 in trophoblast induces the stress activated protein kinase ( SAPK) signal transduction pathways, JNK ( c-Jun-N-Terminal Kinase) and p38, with little induction of the extracellular signal-regulated protein kinase (ERK)-1/2 pathways. Paper-10556174. We found that BMP-7 induced scattering and proinvasive responses (EC50=1 ng/ml) in kidney and colon cancer cell lines through SMAD4 and src -independent pathways and signaling cascades using FAK phosphorylation at Y925 and activation of ERK1/2, Rac1 and JNK. Paper-13312904. Melittin, a major component of bee venom, sensitizes human hepatocellular carcinoma cells to tumor necrosis factor-related apoptosis- inducing ligand (TRAIL)- induced apoptosis by activating CaMKII- TAK1- JNK/ p38 and inhibiting IkappaBalpha kinase-NFkappaB. Paper-13597083. PlGF- induced activation of the SAPK signaling pathways protected trophoblast from growth factor withdrawal-induced apoptosis, but it did not protect trophoblast from apoptosis induced by the pro-inflammatory cytokines, interferon gamma and tumor necrosis factor alpha. Paper-1804302. Here, we demonstrate the involvement of Src protein-tyrosine kinases (PTKs), focal adhesion kinase (FAK), extracellular signal-regulated kinase ( ERK), and c-Jun N-terminal kinase (JNK) but not p38 mitogen- activated protein kinases ( MAPK) in pneumococcal invasion via pIgR. Paper-15498115. LMW-DSP2 dephosphorylated and deactivated p38, to a higher extent, and stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK), but not extracellular signal-regulated kinase 1/2 mitogen-activated protein kinases, in transfected COS7 cells and in vitro. Paper-9019040. TRANCE ( tumor necrosis factor [TNF]-related activation-induced cytokine) is a new member of the TNF family that is induced upon T cell receptor engagement and activates c-Jun N-terminal kinase (JNK) after interaction with its putative receptor (TRANCE-R). Paper-1263546. Upon T-cell receptor stimulation, PKD robustly augments HPK1 kinase activity in Jurkat T cells and enhances HPK1-driven SAPK/JNK and NF-kappaB activation; conversely, antisense down-regulation of PKD results in reduced HPK1 activity. Paper-11169914. The present study used molecular indicators of oxidative stress to place 6-OHDA-generated ROS upstream of the appearance of UPR markers such as activating transcription factor 3 ( ATF3) and phosphorylated stress-activated protein kinase ( SAPK/ JNK) signaling molecules. Paper-12238296. Here we report the identification of a TNF-responsive serine/ threonine protein kinase termed GCK related (GCKR) that likely signals via mitogen-activated protein kinase (MAPK)/extracellular signal- regulated kinase ( ERK) kinase kinase 1 (MEKK1) to activate the SAPK pathway. Paper-1274354. GCDC increased mitogen-activated protein kinase ( MAPK) activity, but had no effect on stress-activated protein kinase ( SAPK) activity in hepatocytes. cAMP decreased basal and GCDC- induced MAPK activity and increased SAPK activity. Paper-1408656. We report that TRAF2, TRAF5 and TRAF6 associate with apoptosis signal-regulating kinase 1 ( ASK1), and a catalytically-inactive ASK1 mutant blocks stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase ( JNK) activation by these TRAFs. Paper-8307443. In both established glioma cell lines and primary glioma cells, apoptosis induced by the inhibition of Rac was partially rescued by activated mitogen-activated protein kinase kinase 1, an activator of JNK, suggesting that JNK functions downstream of Rac1 in glioma cells. Paper-9421188. Interestingly, both constitutive and sIgM-induced phosphorylation of p38 and JNK is inhibited by LAIR-1 through an ITIM-dependent signal, as demonstrated by the use of specific ITIM-binding peptides; importantly, this inhibitory signal is missing when LAIR-1 is not expressed as occurs in HR CLL. Paper-12767454. Transfected MEKK3 has the ability to activate both SAPK and ERK pathways, but does not induce p38 activity, in agreement with a previous report on murine MEKK3 (Blank, J. L., Gerwins, P., Elliott, E. M., Sather, S., and Johnson, G. L. (1996) J. Biol. Chem. 271, 5361-5368). Paper-900260. However, the existence of this inhibitory JNK pathways suggests a mechanism whereby--in the absence of NF-kappaB activation--TNF-alpha production during inflammation in vivo could actually inhibit MUC2 production, giving rise to the defective mucosal protection which characterizes inflammatory bowel disease. Paper-10736785. The inhibition of JNK activity by its specific inhibitor or its dominant negative mutant suppressed both IFIT4 expression and serine phosphorylation of STAT1 but not the activation of PKCdelta, while inhibition of PKCdelta suppressed activation of IFIT4, STAT1, and JNK. Paper-14331818. Our results suggest that the induction of IFIT4 transcription by IFN-alpha depends upon sequential activation of PKCdelta, JNK and STAT1, and that the influence of PKCdelta or JNK on IFN-alpha- mediated induction of IFIT4 is dependent upon the phosphorylation of STAT1 at Ser-727. Paper-14331818. These findings suggest that JNK1 and JNK2 are involved in TNF-alpha- induced neutrophil apoptosis and GM-CSF-mediated antiapoptotic effect on neutrophils, respectively, and both JNK isoforms are involved in TNF-alpha- induced and GM-CSF-induced superoxide release. Paper-14311928. Previous studies have shown that ras- mediated u-PA expression is regulated through the mitogen- ( MAPK) and stress-activated protein kinase ( SAPK) signal transduction pathways extracellular signal-regulated kinase ( ERK) and c-Jun-activating kinase ( JNK). Paper-11243731. Here, we report that Ser-727 phosphorylation of Stat3 can also be induced by JNK and activated either by stress or by its upstream kinase and that various stress treatments induce serine phosphorylation of Stat3 in the absence of tyrosine phosphorylation. Paper-8299703. The JNK pathway is activated in Alzheimer disease (AD), as demonstrated in studies showing higher levels of phospho- JNK in affected neurons in AD brains than in controls. c-Jun, a transcription factor, is the downstream effector of JNK, whose activation requires phosphorylation of Ser63/Ser73. Paper-13253795. MKP-1 blocked the ability of FasL to induce loss of mitochondrial transmembrane potential (delta Psi(m)), suggesting that MKP-1 acts upstream of mitochondrial pro-apoptotic events induced by FasL and that the SAPK/ JNK pathway may form the signaling link between Fas receptor and mitochondrial dysfunction. Paper-8346938. MnTBAP exclusively prevented the phosphorylation of p38 mitogen- activated protein kinase ( MAPK) and stress-activated protein kinase ( SAPK/ JNK) whereas it did not affect the phosphorylation and activation of nuclear factor-kappaB and extracellular signal regulated kinase 1/2. Paper-13117271. The JNK inhibitor SP600125 was used as a demonstration compound because in addition to inhibiting nuclear accumulation of phosphorylated c-Jun it reduced nuclear translocation of phosphorylated p38 and NFkappaB p65/RelA in a dose-dependent manner, indicating a lack of SP600125 selectivity. Paper-11481870. Moreover, peptide versions of any of the three D-sites of MKK7 inhibited the ability of JNK1 and JNK2 to phosphorylate their transcription factor substrates c-Jun and ATF2, suggesting that D-site-containing substrates also compete with MKK7 for docking to JNK. Paper-11845266. Using selective enzyme inhibitors, overexpression of dominant-negative Akt, and Akt siRNA, it was demonstrated that GIP promoted beta-cell survival via Akt-dependent suppression of p38 MAPK and JNK and that combined inhibition was sufficient to explain the entire pro-survival responses to GIP during STS treatment. Paper-14067494. Taken together, our results support a model in which Akt2 binds to a POSH-MLK-MKK- JNK complex and phosphorylates MLK3; phosphorylation of MLK3 by Akt2 results in the disassembly of the JNK complex bound to POSH and down-regulation of the JNK signaling pathway. Paper-10041354. We have previously reported that the basic fibroblast growth factor (FGF-2) stimulates the synthesis of the vascular endothelial growth factor ( VEGF) at least in part via the p44/p42 mitogen- activated protein (MAP) kinase and the stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK) in osteoblast-like MC3T3-E1 cells. Paper-15803216. Overexpression of cyclin D1 protein stimulated by B[a]P was significantly inhibited by 50 microM AG126 (an inhibitor of ERK1/2), but not by 25 microM SP600125 (an inhibitor of JNK1/2) or 5 microM SB203580 (an inhibitor of p38 mapk), suggesting that B[a]P-induced cyclin D1 expression was only regulated by ERK1/2 pathway. Paper-12144428. This was supported by RNA interference where co-transfection of small interfering RNA targeting both JNK1 and JNK2, to limit signaling redundancy, significantly inhibited IL-1alpha-stimulated translocation of phosphorylated c-Jun without altering phosphorylated p38 and NFkappaB p65/RelA redistribution. Paper-11481870. These findings indicate that JNK1- and JNK2-mediated signaling plays a positive and a negative role, respectively, in LPS-induced IL-12 production and PI3K p110beta controls LPS- induced JNK1 activation, not JNK2 activation, resulting in the positive regulation of IL-12 production in THP-1 macrophage cells. Paper-15212050. Furthermore, PKCdelta-mediated activation of STAT1 required the activation of JNK, as the inhibition of JNK activity by its specific inhibitor or transfection of its dominant negative mutant suppressed both serine phosphorylation of STAT1 and PLSCR1 expression but not the activation of PKCdelta. Paper-11006859. CONCLUSIONS: These results suggest that ERK and JNK pathways are involved in PMA- mediated MD-2 gene expression during HL-60 cell differentiation, and the activation of the MEK/possible ERK/Elk signal pathway is the mechanism responsible for PMA-induced MD-2 gene expression in differentiated HL-60 cells. Paper-14320785. RhoB induction by gamma-radiation occurred at the transcriptional level and transcriptional activation of RhoB was concomitant with an increase in RhoB protein. gamma-Radiation- induced RhoB expression was markedly attenuated by pretreatment with a JNK-specific inhibitor, SP600125, but not by a p38 MAPK inhibitor, SB203580. Paper-14222218. Activation of JNK and its downstream caspase-3 by paclitaxel or vinblastine is significantly down-regulated in gamma-synuclein-expressing cells, indicating that the paclitaxel- or vinblastine-activated apoptosis pathway is blocked by gamma-synuclein. Paper-9170460. We therefore propose that leukemic cell survival depends on the maintenance of an imbalance of the outputs from the MAPK and SAPK systems such that the dominant basal influence of the MAPK cascade allows sustained proliferation, whereas acute redirection of this balance toward the SAPK cascade initiates apoptotic cell death. Paper-1282791. Using antibodies which selectively distinguished receptor-regulated Smads (R-Smads) phosphorylated at linker regions from those at C-terminal regions, we herein showed that either HGF or TGF-beta treatment of normal stomach-origin cells activated the JNK pathway, thereafter inducing endogenous R-Smads phosphorylation at linker regions. Paper-10646972. The increase in p21 stability was detected following activation of p38 alpha and JNK1, and treatment of cells with the p38 inhibitor SB203580 prevented this increase in p21 stability. p38 alpha and JNK1 phosphorylated p21 in vivo, and both p38 alpha and JNK1 phosphorylated p21 at Ser(130) in vitro. Paper-9167971. Investigating the molecular basis of activation of the c-Jun N-terminal kinase (JNK) subgroup of MAPK by the MAPKKK MEKK2, we found that strong and specific JNK1 activation by MEKK2 was mediated by the MAPKK JNK kinase 2 ( JNKK2) rather than by JNKK1 through formation of a tripartite complex consisting of MEKK2, JNKK2, and JNK1. Paper-2149787. IL-1 beta- induced uPA protein and mRNA expression in a time- and concentration-dependent manner, which was inhibited by pretreatment with the inhibitors of JNK1/2 (SP600125), PKC (Ro31-8220, Gö6976), or NF-kappaB (helenalin), and transfection with dominant negative mutants of PKC alpha, NIK, and IKK beta, and siRNAs of JNK1/2 and p65. Paper-13590703. When the MCF-7 cells were treated with 200 micromol x L DADS, the stress-activated protein kinase extracellular signal- regulated kinase ( ERK), a mitogen-activated protein kinase, was inhibited after 6 h; c-Jun N-terminal kinase (JNK), that is stress-activated protein kinase ( SAPK), and p38 mitogen-activated protein kinase were activated after 6 h. Paper-13012197. Treatment with an MEK [MAPK (mitogen-activated protein kinase)/ERK (extracellular-signal-regulated kinase) kinase] inhibitor (PD98059) and a JNK ( c-Jun N-terminal kinase) inhibitor (SP600125) suppresses PMA- induced MD-2 gene expression, whereas impairment of p38 function by treatment with the inhibitor SB203580 has no effect on MD-2 mRNA. Paper-14320785. Engagement of CD40 by CD154 stimulated interleukin-8 ( IL-8) and monocyte chemoattractant protein-1 ( MCP-1) production, which proceeded via receptor activation of the extracellular signal-regulated kinase (ERK)1/2, stress-activated protein kinase (SAPK)/c-Jun NH(2)-terminal kinase (JNK), and p38 mitogen-activated protein kinase ( MAPK) pathways. Paper-9452429. Since there are several AP-1 sites in the VEGF promoter, and the c-Jun/ AP-1 is activated through stress-activated protein kinase/ c-Jun N-terminal kinase ( SAPK/ JNK) and extracellular signal regulated kinase ( ERK), we further examined the c-Jun, JNK and ERK that might be involved in the VEGF induced by HBO. Paper-11349116. Stress-activated protein kinase ( SAPK) pathway- regulating phosphatase 1 ( SKRP1) has been identified as a member of the mitogen-activated protein kinase ( MAPK) phosphatase (MKP) family that interacts physically with the MAPK kinase (MAPKK) MKK7, a c-Jun N-terminal kinase (JNK) activator, and inactivates the MAPK JNK pathway. Paper-9165110. Tumor necrosis factor signaling to stress-activated protein kinase (SAPK)/Jun NH2-terminal kinase ( JNK) and p38. Germinal center kinase couples TRAF2 to mitogen-activated protein kinase/ ERK kinase kinase 1 and SAPK while receptor interacting protein associates with a mitogen-activated protein kinase kinase kinase upstream of MKK6 and p38. Paper-1554470. These synonyms are used for gene MAPK8 (mitogen-activated protein kinase 8): Stress-activated protein kinase JNK1, Stress-activated protein kinase 1, SAPK1, PRKM8, Mitogen-activated protein kinase 8, MAP kinase 8, MAPK 8, JNK-46, JNK21B1/2, JNK1A2, JNK1, JNK, c-Jun N-terminal kinase 1. These accession numbers are used for gene MAPK8: U35004 (NCBI_GENBANK__AC), BC144063 (NCBI_GENBANK__AC), B5BUB8 (UNIPROT__AC), A6NF29 (UNIPROT__AC). MAPK8 is a homologue of mapk8b (mitogen-activated protein kinase 8b) from Danio rerio. MAPK8 is a homologue of mapk8a (mitogen-activated protein kinase 8a) from Danio rerio. MAPK8 is a homologue of MAPK8 (mitogen-activated protein kinase 8) from Pan troglodytes. MAPK8 is a homologue of MAPK8 (mitogen-activated protein kinase 8) from Canis lupus familiaris. MAPK8 is a homologue of MAPK8 (mitogen-activated protein kinase 8) from Bos taurus. MAPK8 is a homologue of MAPK8 (mitogen-activated protein kinase 8) from Gallus gallus. MAPK8 is a homologue of Mapk8 (mitogen-activated protein kinase 8) from Mus musculus. MAPK8 is a homologue of Mapk8 (mitogen-activated protein kinase 8) from Rattus norvegicus. MAPK8 is a homologue of LOC100333971 (Mitogen-activated protein kinase 8B-like) from Danio rerio. Important links ! iHOP - Information Hyperlinked over Proteins . Concept & Implementation by Robert Hoffmann.