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Synuclein-positive neurons were negative to ubiquitin and PHF-tau. Paper-9674518.
Disease-related modifications in tau affect the interaction between Fyn and Tau. Paper-10974380.
Effect of Pin1 or microtubule binding on dephosphorylation of FTDP-17 mutant Tau. Paper-13838442.
Regulation of tubulin, Tau and microtubule associated protein 2 expression during mouse brain development. Paper-91193.
In this work we show that BAG-1 associates with Tau protein in an Hsc70-dependent manner. Paper-12644839.
Also an increased binding of phospho-GSK-3beta with phospho- Tau was observed in these WOX1 knock-down cells. Paper-10346132.
Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease. Paper-13933707.
Changes in Tau, cofilin, and other proteins recapitulated abnormalities observed in neurodegenerative states in vivo. Paper-10309850.
Ectopic or endogenous WOX1 colocalized with Tau, JNK1, and GSK-3beta in neurons and cultured cells. Paper-10346132.
Finally, BAG-1 is highly expressed in neurons bearing Tau tangles in a mouse model of Alzheimer disease. Paper-12644839.
Here we demonstrate that Fyn binds to the cytoskeletal proteins Tau and alpha-Tubulin in oligodendrocytes. Paper-9367490.
The observations on Tau protein were replicated in cell lines using laforin overexpression and knockdown approaches. Paper-13933707.
Cdk5 is involved in NFT-like tauopathy induced by transient cerebral ischemia in female rats. Paper-12458948.
Memory and exploratory impairment in mice that lack the Park-2 gene and that over- express the human FTDP-17 mutant Tau. Paper-14393740.
BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. Paper-12644839.
Overexpression of BAG-1 induced an increase in Tau levels, which is shown to be due to an inhibition of protein degradation. Paper-12644839.
They were immunoreactive for the microtubule-associated protein tau and the lysosomal-associated membrane protein 1 ( LAMP1). Paper-14207166.
Glycogen synthase kinase-3beta (GSK-3beta), antagonized by protein phosphatase 2A ( PP2A), regulates Tau phosphorylation at many sites. Paper-12673906.
Continuous addition of NeuroD2 protein resulted in N1E-115 cells adopting neural morphology after 4 days and Tau mRNA expression was increased. Paper-12276311.
Dephosphorylation of wild-type Tau was reduced in brain extracts of Pin1-knockout mice, and this reduction was not observed with P301L and R406W. Paper-13838442.
The mutant Tau protein binds to the Fyn SH3 domain but lacks the microtubuli interaction domain and thus cannot bind to microtubuli. Paper-9367490.
We also show here that laforin and Tau proteins physically interact and that the interaction was limited to the phosphatase domain of laforin. Paper-13933707.
This review summarizes recent evidence suggesting that caspase cleavage of tau plays an important role in the development of neurofibrillary tangle pathology. Paper-10802487.
Recent evidence suggests that microtubule-associated protein tau may mediate amyloid-β peptide (Aβ) toxicity by modulating the tyrosine kinase Fyn. Paper-15616694.
These balanced responses seem to ensure the steady Tau phosphorylation at GSK/ PP2A-dependent sites observed over a long period of time (>/=6 h). Paper-12673906.
Finally, our in vitro and in vivo assays demonstrate that laforin dephosphorylates Tau, and therefore laforin is a novel Tau phosphatase. Paper-13933707.
RNA-mediated interference depletion of BAG-1 leads to a decrease in total Tau protein levels as well as promoting hyperphosphorylation of the remaining protein. Paper-12644839.
We studied the effect of the peptidyl-prolyl isomerase Pin1 or microtubule binding on dephosphorylation of wild-type Tau, P301L, and R406W in vitro. Paper-13838442.
Enhanced neurofibrillary tangle formation, cerebral atrophy, and cognitive deficits induced by repetitive mild brain injury in a transgenic tauopathy mouse model. Paper-11166238.
However, because Hsp70/ Hsc70 has many binding partners that can mediate its activity, there is still much to discover about how Hsp70 acts in vivo to regulate Tau protein. Paper-12644839.
We further show that BAG-1 can inhibit the degradation of Tau protein by the 20 S proteasome but does not affect the ubiquitination of Tau protein. Paper-12644839.
3. Tau proteins begin to be detected at postnatal day 8 in the molecular layer but only at the level of the parallel fibers that are present in the Purkinje cell dendritic field. Paper-27375.
The 5' and 3' flanking genes for MAPT are the corticotrophin- releasing factor receptor (CRFR) gene and KIAA1267, a gene of unknown function expressed in brain. Paper-8959129.
ILK inactivation resulted in an increase in the active form but a decrease in the inactive form of GSK-3beta, which is a candidate kinase involved in PHF-tau formation. Paper-9793328.
Down-regulation of WW domain-containing oxidoreductase induces Tau phosphorylation in vitro. A potential role in Alzheimer's disease. Paper-10346132.
Conclusions: Our current findings are the first to show that overexpression of Tau-P301S in adult mice overexpressing APP, but not wild-type mice, leads to enhanced Tau-related pathology. Paper-12764968.
Aims: In this study, we aimed to investigate the interaction between amyloid- and Tau-associated pathologies to gain further insights into the development of Alzheimer's disease. Paper-12764968.
This effect is likely to be caused by interference with the Fyn-Tau-microtubuli cascade rather than inactivation of the kinase, because Fyn bound to the mutant Tau retains activity. Paper-9367490.
The level of three microtubule proteins, tubulin, Tau and MAP2 and of their encoding mRNA was studied in the mouse brain at an early developmental stage (3 days postnatal) and in adulthood. Paper-91193.
Induction of Hsp70 by heat shock enhanced the increase of Tau levels in cells overexpressing BAG-1 but induced a decrease of Tau levels in cells that were depleted of BAG-1. Paper-12644839.
To study the function of the Fyn- Tau interaction in oligodendrocytes, we designed a Tau deletion mutant that would compete with endogenous Tau- Fyn binding in transfected cells. Paper-9367490.
Hsp70/ Hsc70, a member of the chaperone protein family, interacts with Tau protein and mediates proper folding of Tau and can promote degradation of Tau protein under certain circumstances. Paper-12644839.
RESULTS: Gosr2, Wnt9b, Wnt3, Nsf, Arf2, Crhr1, Mapt, Cdc27, Myl4, Itgb3, chr11_20.152, chr11_20.154, chr11_20.155, and chr11_20.156 are expressed in ED10-11 heads. Paper-10974803.
Expression correlation and genetic network analysis demonstrated that Mapt co-varies with many tauopathies-related genes, including Gsk3b, Falz, Apbb2, Slc1a3, Ntrk2, Pik3ca, and Ikbkap. Paper-13893673.
Together WOX1 binds Tau via its short-chain alcohol dehydrogenase/reductase domain and is likely to play a critical role in regulating Tau hyperphosphorylation and NFT formation in vivo. Paper-10346132.
We examined the formation of neurofibrillary tangles (NFT) in adult mouse brain without the prior overexpression of Tau at embryonic or early post-natal stages to dissociate any developmental mechanisms. Paper-12764968.
Our analyses on the Epm2a gene knock-out mice, which developed most of the symptoms of LD, reveal the presence of hyperphosphorylated Tau protein (Ser(396) and Ser(202)) as neurofibrillary tangles (NFTs) in the brain. Paper-13933707.
Hippocampal samples taken from FAD mutant (I213T) PS1 knock-in mice contained hyperphosphorylated tau that reacted with various phosphodependent tau antibodies and with Alz50, which recognizes the conformational change of PHF tau. Paper-11317192.
Second, humanized MAPT transgenic mice lacking CX3CR1 exhibited enhanced MAPT phosphorylation and aggregation as well as behavioral impairments that correlated with increased levels of active p38 MAPK. Paper-15394632.
17Beta-estradiol, a neuronal protective hormone, increased the binding of WOX1 and GSK-3beta with Tau. Mapping analysis showed that WOX1 bound Tau via its COOH-terminal short-chain alcohol dehydrogenase/reductase domain. Paper-10346132.
Activation of JNK1 by anisomycin further increased Tau phosphorylation, and SP600125 (a JNK inhibitor) and PD-98059 (an MEK1/2 inhibitor) blocked Tau phosphorylation and NFT formation in these WOX1 knock-down cells. Paper-10346132.
Taken together, our study suggests that laforin is one of the critical regulators of Tau protein, that the NFTs could underlie some of the symptoms seen in LD, and that laforin can contribute to the NFT formation in Alzheimer disease and other tauopathies. Paper-13933707.
Because ligation of the cell adhesion molecule F3 on oligodendrocytes leads to activation of Fyn kinase localized in rafts, these findings suggest that recruitment of Tau and Tubulin to activated Fyn kinase in rafts is an important step in the initiation of myelination. Paper-9367490.
These mice develop both amyloid plaques and neurofibrillary tangle-like pathology in a progressive and age-dependent manner, while these pathological hallmarks are predominantly restricted to the hippocampus, amygdala, and the cerebral cortex the main foci of AD neuropathology in humans. Paper-12982434.
On the other hand, the investigation of Tau protein at Ser-262 showed that interference in the insulin/ PI3K and mTor signaling potentially influenced the Tau phosphorylation status at sites where only one of two enzymes (in this case PP2A) is involved in the regulation. Paper-12673906.
Remarkably knock-down of WOX1 expression by small interfering RNA in neuroblastoma SK-N-SH cells spontaneously induced Tau phosphorylation at Thr212/Thr231 and Ser515/Ser516, enhanced phosphorylation of glycogen synthase kinase 3beta (GSK-3beta) and ERK, and enhanced NFT formation. Paper-10346132.
With this evidence we continued to explore the regulation of CTGF in postmortem AD brain tissue and found that CTGF expression correlated with the progression of AD clinical dementia and amyloid neuritic plaque (NP) neuropathology, but not neurofibrillary tangle ( NFT) deposition. Paper-10775456.
Tau-tubulin kinase-1 ( TTBK1) phosphorylates microtubule-associated protein tau at specific serine/ threonine residues found in paired helical filaments (PHFs), and its expression is up-regulated in the brain in Alzheimer disease, suggesting its role in tauopathy pathogenesis. Paper-15182197.
Stable transfection of a kinase-deficient ILK mutant (DN- ILK) resulted in aberrant tau phosphorylation in N1E-115 cells at sites recognized by the Tau-1 antibody that are identical to some of the phosphorylation sites in paired helical filaments, PHF-tau, in brains of patients with Alzheimer's disease. Paper-9793328.
First, lipopolysaccharide-induced microglial activation promotes hyperphosphorylation of endogenous mouse MAPT in nontransgenic mice that is further enhanced in mice lacking the microglial-specific fractalkine receptor ( CX3CR1) and is dependent upon functional toll-like receptor 4 and interleukin-1 (IL-1) receptors. Paper-15394632.
At the same time, Tau-P301LxGSK-3B mice have dramatic forebrain tauopathy, with "tangles in almost all neurons", although without hyper-phosphorylation of Tau. The data corroborate the hypothesis that GSK-3B is the missing link between the amyloid and tau-pathology, and position GSK-3B as prominent player in the pathogenesis in AD. Paper-12262273.
TAPP and JNPL3 mice were studied with immunocytochemistry and immunoblotting with antibodies to glycogen synthase kinase-3 (GKS3) to determine whether the development of tauopathy is associated with activation or increased expression of GSK3, and when the observed changes occur with respect to neurofibrillary tangle ( NFT) formation. Paper-10028710.
As a potential underlying mechanism, we were able to determine that transient ischemia induced tau hyperphosphorylation and NFT-like conformations are associated with aberrant activation of cyclin dependent kinase 5 ( Cdk5) and can be rescued by delivery of a potent, but non-specific cyclin dependent kinase inhibitor, roscovitine to the brain. Paper-12458948.
These synonyms are used for gene Mapt (microtubule-associated protein tau): Tau, PHF-tau, Paired helical filament-tau, Neurofibrillary tangle protein, Mtapt, Microtubule-associated protein tau, AW045860, AI413597.
These accession numbers are used for gene Mapt: Q60686 (UNIPROT__AC), Q60685 (UNIPROT__AC), CO432693 (NCBI_GENBANK__AC), AF483518 (NCBI_GENBANK__AC).
Mapt is a homologue of mapta (microtubule-associated protein tau a) from Danio rerio.
Mapt is a homologue of MAPT (microtubule-associated protein tau) from Bos taurus.
Mapt is a homologue of MAPT (microtubule-associated protein tau) from Gallus gallus.
Mapt is a homologue of Mapt (microtubule-associated protein tau) from Rattus norvegicus.
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iHOP - Information Hyperlinked over Proteins .
Concept & Implementation by Robert Hoffmann.