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Suppressing the expression of all tau isoforms disrupted only those neuronal microtubules containing class II beta-tubulin (show TUBB Proteins), and that boosting the expression of the largest 'big', but not the smallest, tau isoform enhanced neurite outgrowth.
Pin1 (show PIN1 Proteins) serves as a positive regulatory molecule of proplatelet formation of megakaryocytes by enhancing the function of phosphorylated tau.
Here, the authors identify another Wnt (show WNT2 Proteins) signaling amplifier, CKIepsilon (show CSNK1E Proteins), which is specifically upregulated in intestinal stem cells and is essential for intestinal stem cell maintenance, especially in the absence of its close isoform CKIdelta (show CSNK1D Proteins).
PGRN (show GRN Proteins) decrease, resulting from pathogenic mutations, might compromise the trophism of cortical neurons by affecting GluN2B (show GRIN2B Proteins)-contaning NMDA receptors
These results suggest that tau haploinsufficiency, without the compensation effect of MAP1A (show MAP1A Proteins), induces reduction of Otx2 (show OTX2 Proteins) expression, increases prenatal cell death, and accordingly leads to selective loss of VTA DA neurons in the early postnatal stage.
High-glucose induces tau hyperphosphorylation through activation of TLR9 (show TLR9 Proteins)-P38 MAPK (show MAPK14 Proteins) pathway.
these results uncover a novel role for mDia1 in Abeta-mediated synaptotoxicity and demonstrate that inhibition of MT dynamics and accumulation of PTMs are driving factors for the induction of tau-mediated neuronal damage.
The authors show here that miR (show MLXIP Proteins)-132 loss exacerbates both amyloid and TAU pathology via inositol 1,4,5-trisphosphate 3-kinase B (ITPKB (show ITPKB Proteins)) upregulation in an Alzheimer's disease mouse model.
TIA1 (show TIA1 Proteins) knockdown or knockout inhibits tau misfolding and associated toxicity in cultured hippocampal neurons, while overexpressing TIA1 (show TIA1 Proteins) induces tau misfolding and stimulates neurodegeneration.
Data suggest that a switch in post-translational processing of Tau from acetylation at Lys321 to phosphorylation at Ser324 coordinately regulates Tau aggregation and may be relevant in tauopathy and Alzheimer disease; acetylation/phosphorylation of Tau appears to be controlled by Hdac6 (histone deacetylase 6 (show HDAC6 Proteins) protein).
ROS produced by 1,2-diacetylbenzene causes tau hyperphosphorylation via GSK-3beta phosphorylation and it might be related to impaired memory deficit.
Results demonstrate a strong association between progranulin (show GRN Proteins) deficiency and reduction of Tau protein expression that could lead to severe neuronal and glial dysfunctions; also indicate that this frontotemporal lobar degeneration (FTLD)-TDP-GRN (show GRN Proteins) subgroup could be part as a distinct entity of FTLD classification.
Study identified the binding site between tau and fyn (show FYN Proteins)-SH3 may facilitate the development of compounds that can inhibit tau-fyn (show FYN Proteins) interactions, which presents an alternative therapeutic strategy for Alzheimer's disease; and provide evidence that a physiological correlation between phosphorylated tau at S202, S262, and S396/404 and fyn (show FYN Proteins) is not present in Alzheimer's disease brain.
The results emphasize an additional level of complexity in the regulation of the interaction between BIN1 (show BIN1 Proteins) and Tau dependent on the BIN1 (show BIN1 Proteins) isoforms.
There is a link between regional MAPT expression and selective vulnerability of functional brain networks to neurodegeneration.
TDP-43 (show TARDBP Proteins) suppressed tau expression by promoting its mRNA instability through the UG repeats of its 3-UTR. Neurodegenerative diseases-causing TDP-43 (show TARDBP Proteins) mutations affected tau mRNA instability differentially, in that some promoted and others did not significantly affect tau mRNA instability.The level of TDP-43 (show TARDBP Proteins), which is decreased in AD brains, was found to correlate negatively with the tau level in human brain.
Data show that cyclophilin 40 (CyP40) interacts with and dissolves amyloids forming proteins tau and alpha-synuclein aggregates.
results show that neuroinflammation promotes neuronal autophagy and that chronic mild TLR4 (show TLR4 Proteins) stimulation attenuates Alzheimer's disease-related tauopathy, likely by activating neuronal autophagy
Mutation of MAPT is a common cause of FTD (show FTL Proteins) in mainland China.
Data suggest that a switch in post-translational processing of Tau from acetylation at Lys321 to phosphorylation at Ser324 coordinately regulates Tau aggregation and may be relevant in tauopathy and Alzheimer disease; acetylation/phosphorylation of Tau appears to be controlled by HDAC6 (histone deacetylase 6 (show HDAC6 Proteins) protein).
The data of this study provided strong evidence that soluble forms of tau and Abeta (show APP Proteins) co-localise early in AD and are closely linked to disease progression and cognitive decline.
Findings suggest that the endothelin-1 (show EDN1 Proteins)-induced down-regulation of NaV1.7 (SCN9A (show SCN9A Proteins)) diminishes NaV1.7 (show SCN9A Proteins)-related catecholamine secretion and dephosphorylation of tau.
The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn (show FYN Proteins).
show that cathepsin D (show CTSD Proteins) cleaves both tau and beta-amyloid precursor protein (APP). Both tau and APP (show APP Proteins) are involved in the pathogenesis of Alzheimer's disease
results suggest that Nav1.7-Ca2+ influx-protein kinase C-alpha pathway activated ERK1/ERK2 and p38, which increased phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation
We conclude that GSK3beta phosphorylates tau directly at S(202) but requires the previous phosphorylation on S(235) to phosphorylate T(231). Phosphorylation of S(396), on the other hand, occurs sequentially.
age-related increase in cAMP-dependent protein kinase (show CDK7 Proteins) (PKA) phosphorylation of tau at serine 214 (pS214-tau) in monkey dorsolateral prefrontal association cortex specifically targets spine synapses and the Ca(2 (show CA2 Proteins)+)-storing spine apparatus.
We found that inversion of the MAPT region is similarly polymorphic in other great ape species, and we present evidence that the inversions occurred independently in chimpanzees and humans
This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
, tau-like protein-2
, microtubule-associated protein tau
, Microtubule-associated protein tau
, CKI, epsilon
, KC1 epsilon
, casein kinase I isoform epsilon
, G protein beta1/gamma2 subunit-interacting factor 1
, neurofibrillary tangle protein
, paired helical filament-tau
, microtubule associated protein tau
, Neurofibrillary tangle protein
, Paired helical filament-tau
, Tau microtubule-associated protein