Click here for the function of MAPRE1.
Edit this page in Wiki Genes - MAPRE1 or see Wiki Gene.
MCAK associates with EB1. Paper-14400728.
Structural insights into the EB1- APC interaction. Paper-10782176.
APC binds to the novel protein EB1. Paper-288962.
Microtubule plus-end tracking by CLIP-170 requires EB1. Paper-13574816.
In contrast, CLIP-170 does not end-track by itself but requires EB1. Paper-13520142.
Regulation and function of the interaction between the APC tumour suppressor protein and EB1. Paper-2183708.
However, it is largely unknown whether the EB1- APC interaction affects microtubule dynamics. Paper-8851577.
These results suggest that the interaction of EB1 and APC is important and may be conserved. Paper-8851577.
We have also found that the CDK5RAP2- EB1 complex regulates microtubule dynamics and stability. Paper-13934094.
In vitro interaction studies confirmed that the APC basic domain did not contribute to EB1 binding. Paper-2183708.
Targeting of KIF17 to plus ends of growing MTs requires kinesin motor activity and interaction with EB1. Paper-15354512.
APC and EB1 function together in mitosis to regulate spindle dynamics and chromosome alignment. Paper-11301261.
We show that MCAK associates with the C-terminus of EB1 and EB3 but much less efficiently with RP1. Paper-14400728.
Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Paper-8851577.
Knockdown of EB1 expression using siRNA impaired the ability of GFP- MCAK to localize to MT tips in transfected cells. Paper-14400728.
In addition, EB1 is controlled by c-Myc, RhoA, and CDC42, which have all been linked to HCC malignancy. Paper-13473160.
CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex. Paper-10742333.
The adenomatous polyposis coli- binding protein EB1 is associated with cytoplasmic and spindle microtubules. Paper-1558948.
EB1 also interacts with the plus-ends of microtubules and targets APC to microtubule tips. Paper-8851577.
Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics. Paper-13934094.
Proteomic profiling reveals the prognostic value of adenomatous polyposis coli- end-binding protein 1 in hepatocellular carcinoma. Paper-13473160.
Significantly, this C- APC activity is abolished by phosphorylation, which also disrupts its ability to bind to EB1. Paper-8851577.
Therefore, EB1 appeared to be co-localized and interact with APC on the growing ends of a subset of microtubules. Paper-8423432.
CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/ tubulin-binding sites. Paper-13520142.
The APC- associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain. Paper-1844984.
The characteristics of the adenomatous polyposis coli ( APC) associated protein EB1 were examined in mammalian cells. Paper-1751688.
Pin2/ TRF1 bound EB1 both in vitro and in vivo and they also co-localize at the mitotic spindle in cells. Paper-9153097.
Here we characterized a new Pin2/ TRF1-interacting protein, EB1, that was originally identified in our yeast two-hybrid screen. Paper-9153097.
Confocal microscopy demonstrated that exogenous EB3, like EB1, is associated with the cytoplasmic microtubule network. Paper-2096503.
Immunoprecipitation suggested that APC and EB1 were not associated in cultures of HCT116 cells arrested in mitosis. Paper-2183708.
Furthermore, EB1 inhibits the ability of Pin2/ TRF1 to promote microtubule polymerization in vitro. Paper-9153097.
Human EB1 was originally cloned as a protein that interacts with the COOH terminus of adenomatous polyposis coli ( APC). Paper-8851577.
Conclusion: Proteomic profiling revealed the molecular signature behind the progression of HCC, and the prognostic value of EB1 in HCC. Paper-13473160.
EB1 associates with the N-terminal localization and regulatory domain in MCAK but not with the motor domain of the protein. Paper-14400728.
In agreement with the mutational analysis, suppression of EB1 expression inhibits microtubule tip-tracking of CDK5RAP2. Paper-13934094.
The interaction between the adenomatous polyposis coli ( APC) tumour suppressor and the microtubule- associated protein EB1 was examined. Paper-2183708.
Here we used a combination of methods to investigate the dimerization properties of the three human EB proteins EB1, EB2, and EB3. Paper-14248175.
To examine the interaction between APC and EB1 within cells, we compared the dynamic behavior of EB1-GFP with that of APC-GFP in A6 transfectants. Paper-8423432.
Here, we confirm that human MCAK colocalizes with EB1 at growing MT ends when expressed as a GFP fusion protein in transfected cells. Paper-14400728.
KIF17 stabilizes microtubules and contributes to epithelial morphogenesis by acting at MT plus ends with EB1 and APC. Paper-15354512.
Here, we show that TIP150 is a new +TIP that binds to end-binding protein 1 (EB1) in vitro and co-localizes with EB1 at the MT plus ends in vivo. Paper-13908434.
Protein depletion and rescue experiments showed that EB1 and EB3, but not EB2, promote persistent microtubule growth by suppressing catastrophes. Paper-13656721.
We also determined that the EB1 family protein-binding regions are amino acids 2781-2820 and 18-111 of APC and p150glued, respectively. Paper-10041060.
This conservation suggests an essential function for EB1 that might provide clues to the mechanism through which APC suppresses colonic neoplasia. Paper-288962.
EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue. Paper-2096503.
CLIP-170 recognizes and turns over rapidly on composite binding sites constituted by end-accumulated EB1 and tyrosinated alpha-tubulin. Paper-13520142.
These findings showed that the APC- EB1 interaction is regulated within cells and is allowed near the ends of microtubules only under restricted conditions. Paper-8423432.
Furthermore, yeast EB1 protein effectively substitutes for the human protein but also requires C- APC in promoting microtubule polymerization. Paper-8851577.
EB1, which was identified as an APC-binding protein by yeast two-hybrid analysis [5], was also reported to be associated with microtubules [6] [7] [8]. Paper-8423432.
We have found that the C-terminal 50 and 84 amino acids (aa) of EB1 were sufficient to mediate the interactions with APC and dynactin, respectively. Paper-9635548.
Given that EB1 is a microtubule plus end-binding protein, these results further confirm a specific interaction between Pin2/ TRF1 and the mitotic spindle. Paper-9153097.
EB1 formed mutually exclusive complexes with APC and dynactin, and a direct interaction between EB1 and p150(Glued) was identified. Paper-9635548.
EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle. Paper-1751688.
We show now that RP1 and the other known members of the EB/RP family ( EB1 and RP3) also bind directly to tubulin, both in vitro and in vivo. Paper-1786564.
Collectively, these results show that CDK5RAP2 targets growing microtubule tips in association with EB1 to regulate microtubule dynamics. Paper-13934094.
EB1 family proteins use overlapping but different regions that contain the EB1-like C-terminal motif to associate with APC and p150glued. Paper-10041060.
The previously described puncta of the APC protein at the leading edge of membrane protrusions contact microtubule fibers that contain RP1 or EB1. Paper-1786564.
EB1 is a microtubule tip- associated protein that interacts with the APC tumor suppressor protein and components of the dynein/ dynactin complex. Paper-9635548.
The association of EB1 with members of the dynactin complex was independent of APC and was preserved in the absence of an intact microtubule cytoskeleton. Paper-1844984.
Immunohistochemical analyses reveal a distinct staining pattern during interphase as well as an association of RP1/ EB1 with mitotic microtubule structures. Paper-1786564.
Phosphorylation of the conserved Cdc2 site Ser2789-Lys2792 in C-APCp1 reduces binding four-fold, indicating that the interaction APC- EB1 is post-translationally regulated in cells. Paper-10782176.
Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. Paper-13163082.
Thus, the interaction between EB1 and APC plays an essential role in the regulation of microtubule polymerization, and a similar mechanism may be conserved in yeast. Paper-8851577.
Among several cDNA clones we isolated from a fetal-brain cDNA library as candidates, six included an identical sequence with significant homology to EB1, a protein known to bind to APC. Paper-2096503.
We reconstituted the +TIP tracking of mammalian proteins EB1 and CLIP-170 in vitro at single-molecule resolution using time-lapse total internal reflection fluorescence microscopy. Paper-13574816.
The CDK5RAP2- EB1 complex induces microtubule bundling and acetylation when expressed in cell cultures and stimulates microtubule assembly and bundle formation in vitro. Paper-13934094.
Here, we reconstitute a vertebrate plus end tracking system composed of the most prominent +TIPs, end-binding protein 1 ( EB1) and CLIP-170, in vitro and dissect their end-tracking mechanism. Paper-13520142.
The EB1- binding motif is conserved in the CDK5RAP2 sequences of chimpanzee, bovine, and dog but not in those of rat and mouse, suggesting a function gained during the evolution of mammals. Paper-13934094.
The C-terminal 170 amino acids of APC, purified as a bacterial fusion protein, precipitated EB1 from cell extracts, significantly refining the location of the EB1 interaction domain in APC. Paper-2183708.
In yeast, EB1 regulates microtubule dynamics, and its binding domain in APC may be conserved in Kar9, an EB1 binding protein involved in the microtubule-capturing mechanism. Paper-8851577.
Here, we examine the possibility that APC mutants interfere with the function of EB1, a plus-end microtubule-binding protein that interacts with APC and is required for normal microtubule dynamics. Paper-11301261.
The full-length cDNA of this novel homologue of EB1, named EB3, encoded a protein of 282 amino acids with 54% identity to EB1, and it was expressed preferentially in brain tissue on Northern blots. Paper-2096503.
EB1 proteins bind to microtubule ends where they act in concert with other components, including the adenomatous polyposis coli ( APC) tumor suppressor, to regulate the microtubule filament system. Paper-10782176.
Neither APC nor p150glued binding domain is necessary for EB1 or EBF3 to induce microtubule bundling, which requires amino acids 1-181 and 1-185 of EB1 and EBF3, respectively. Paper-10041060.
Among the proteins identified, we focused on APC-binding protein EB1 ( EB1) because it was dominantly expressed in poorly differentiated HCCs, which generally correlate with the poor prognosis in patients with HCC. Paper-13473160.
CDK5RAP2 interacts directly with EB1, a prototypic member of microtubule plus-end tracking proteins, and contains the basic and Ser-rich motif responsible for EB1 binding. Paper-13934094.
In addition, HDAC6 was found to be physically associated with the microtubule end-tracking protein EB1 and a dynactin core component, Arp1, both of which accumulate at the tips of growing microtubules. Paper-13995854.
Single-molecule analysis of the CLIP-170- EB1 complex also indicates a short dwell time at growing plus-ends, an observation inconsistent with the copolymerization of this complex with tubulin for plus-end-specific localization. Paper-13574816.
Since APC is detected on the kinetochores of chromosomes, it has been hypothesized that the EB1- APC interaction connects microtubule spindles to the kinetochores and regulates microtubule stability. Paper-8851577.
CLIP-170 exhibits lattice diffusion and fails to selectively track microtubule ends in the absence of EB1; the addition of EB1 is both necessary and sufficient to mediate plus-end tracking by CLIP-170. Paper-13574816.
Associating with the mitotic apparatus, EB1 may play a physiologic role connecting APC to cellular division, coordinating the control of normal growth and differentiation processes in the colonic epithelium. Paper-1558948.
Human EB1 is a highly conserved protein that binds to the carboxyl terminus of the human adenomatous polyposis coli ( APC) tumor suppressor protein [1], a domain of APC that is commonly deleted in colorectal neoplasia [2]. Paper-1844984.
Human EB1 family proteins, which include EB1, EBF3, and RP1, also associate with the tumor suppressor protein adenomatous polyposis coli ( APC) and p150glued, a component of the dynactin complex. Paper-10041060.
The association of APC and EB1 proteins was confirmed with in vitro binding assays. mAbs against EB1 were then produced and used to demonstrate the association of APC and EB1 in vivo. Paper-288962.
We show that APC(1-1450) acts as a dominant negative by forming a hetero-oligomer with the full-length APC and preventing it from interacting with EB1, which is consistent with a functional relationship between APC and EB1. Paper-11301261.
Extension of these studies of the EBc domains to full-length EBs demonstrate that heterodimer formation between EB1 and EB3, but not between EB2 and the other two EBs, occurs both in vitro and in cells as revealed by live cell imaging. Paper-14248175.
Expression of GFP fusions to C-terminal APC sequences lacking or including the APC basic domain but encompassing the EB1 binding region in SW480 cells revealed a microtubule tip association which co-localized with that of EB1. Paper-2183708.
Immunostaining of SW480 cells, which contain truncated APC incapable of interaction with EB1, showed that the association of EB1 with microtubules throughout the cell cycle was not dependent upon an interaction with APC. Paper-1751688.
Here, we show that EB1 potently promotes microtubule polymerization in vitro and in permeabilized cells, but, surprisingly, only in the presence of the COOH-terminal EB1 binding domain of APC (C- APC). Paper-8851577.
We show that amino acids 1-133 of EB1 and EBF3 and the corresponding region of RP1, which contain a CH domain, are necessary and sufficient for binding microtubules, thus demonstrating for the first time that a CH domain contributes to binding microtubules. Paper-10041060.
These findings strongly suggest that the interaction between APC and EB1 targets APC to microtubule tips, and that the interaction between the two proteins is down-regulated during mitosis by the previously described mitotic phosphorylation of APC. Paper-2183708.
We propose that MCAK is targeted to growing MT ends by EB1, that MCAK is held in an inactive conformation when associated with EB1 and that this could provide the basis for a mechanism that facilitates rapid switching between phases of MT growth and depolymerization. Paper-14400728.
EB1 was also found associated with the intermediate chain of cytoplasmic dynein (CDIC) and with dynamitin (p50), another component of the dynactin complex, but not with dynein heavy chain, in a complex that sedimented at approximately 5S in a sucrose density gradient. Paper-1844984.
The evolutionarily conserved protein EB1 originally was identified by its physical association with the carboxyl-terminal portion of the adenomatous polyposis coli ( APC) tumor suppressor protein, an APC domain commonly mutated in familial and sporadic forms of colorectal neoplasia. Paper-1558948.
We show that siRNA-mediated inhibition of APC, EB1, or APC and EB1 together give rise to similar defects in mitotic spindles and chromosome alignment without arresting cells in mitosis; in contrast inhibition of CLIP170 or LIS1 cause distinct spindle defects and mitotic arrest. Paper-11301261.
By using live cell experiments and in vitro reconstitution assays, we demonstrate that a short polypeptide motif, Ser-x-Ile-Pro (SxIP), is used by numerous +TIPs, including the tumor suppressor APC, the transmembrane protein STIM1, and the kinesin MCAK, for localization to microtubule tips in an EB1-dependent manner. Paper-13788397.
Immunofluorescence analysis of SW480, a colon cancer cell line that expresses only carboxyl-terminal-deleted APC unable to interact with EB1, demonstrated that EB1 remained localized to the microtubule cytoskeleton, suggesting that this pattern of subcellular distribution is not mediated by its interaction with APC. Paper-1558948.
These synonyms are used for gene MAPRE1 (microtubule-associated protein, RP/EB family, member 1): Microtubule-associated protein RP/EB family member 1, MGC129946, MGC117374, End-binding protein 1, EB1, APC-binding protein EB1.
These accession numbers are used for gene MAPRE1: EU832776 (NCBI_GENBANK__AC), E1P5M8 (UNIPROT__AC), B2R6I7 (UNIPROT__AC), AK310817 (NCBI_GENBANK__AC).
MAPRE1 is a homologue of Os10g0498900 (Os10g0498900) from Oryza sativa Japonica Group.
MAPRE1 is a homologue of NCU00243 (similar to microtubule associated protein EB1) from Neurospora crassa OR74A.
MAPRE1 is a homologue of MGG_05427 (hypothetical protein) from Magnaporthe oryzae 70-15.
MAPRE1 is a homologue of MAPRE1 (microtubule-associated protein, RP/EB family, member 1) from Pan troglodytes.
MAPRE1 is a homologue of MAPRE1 (microtubule-associated protein, RP/EB family, member 1) from Canis lupus familiaris.
MAPRE1 is a homologue of MAPRE1 (microtubule-associated protein, RP/EB family, member 1) from Bos taurus.
MAPRE1 is a homologue of MAPRE1 (microtubule-associated protein, RP/EB family, member 1) from Gallus gallus.
MAPRE1 is a homologue of Mapre1 (microtubule-associated protein, RP/EB family, member 1) from Mus musculus.
MAPRE1 is a homologue of Mapre1 (microtubule-associated protein, RP/EB family, member 1) from Rattus norvegicus.
MAPRE1 is a homologue of mapre1 (microtubule-associated protein, RP/EB family, member 1) from Danio rerio.
MAPRE1 is a homologue of mal3 (EB1 family Mal3) from Schizosaccharomyces pombe 972h-.
MAPRE1 is a homologue of KLLA0B11550g (hypothetical protein) from Kluyveromyces lactis NRRL Y-1140.
MAPRE1 is a homologue of BIM1 (Bim1p) from Saccharomyces cerevisiae S288c.
MAPRE1 is a homologue of ATEB1C (ATEB1C (microtubule end binding protein 1); microtubule binding) from Arabidopsis thaliana.
MAPRE1 is a homologue of AGOS_AAR024W (AAR024Wp) from Ashbya gossypii ATCC 10895.
Important links !
iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.