2.7.11.26 ATP + alpha-actin - 2.7.11.26 ATP + amyloid precursor protein - 2.7.11.26 ATP + beta-catenin - 2.7.11.26 ATP + c-Myc - 2.7.11.26 ATP + CCDC92 - 2.7.11.26 ATP + CEP164 TTBK2-induced phosphorylations of CEP164 modulate its function, which in turn seems relevant for the process of cilia formation 2.7.11.26 ATP + CEP83 - 2.7.11.26 ATP + CEP89 - 2.7.11.26 ATP + cyclin D - 2.7.11.26 ATP + cyclin E - 2.7.11.26 ATP + DVL3 - 2.7.11.26 ATP + glycogen synthase - 2.7.11.26 ATP + mu-calpain - 2.7.11.26 ATP + nuclear factor-kappaB - 2.7.11.26 ATP + p53 - 2.7.11.26 ATP + protein tau - 2.7.11.26 ATP + protein tau prior phosphorylation of tau by isoenzyme TPKII strongly enhances the action of TPKI 2.7.11.26 ATP + protein tau regulates PDH and participates in energy metabolism and acetylcholine synthesis 2.7.11.26 ATP + protein tau microtubule-associated protein 2.7.11.26 ATP + protein tau phosphorylates tau on S202, T231, S396, and S400 but not on S262, S235, and S404. Phosphorylates tau directly at S202 but requires the previous phosphorylation on S235 to phosphorylate T231, once a priming kinase phosphorylates S404, GSK3beta sequentially phosphorylates S400 and then S396 2.7.11.26 ATP + Rabin8 - 2.7.11.26 ATP + SC35 substrate prephosphorylated SC35, SC35 is a member of the SR family of serine/arginine-rich splicing factors 2.7.11.26 ATP + tau protein tau in Alzheimer disease brain is highly phosphorylated and aggregates into paired helical filaments comprising characteristic neurofibrillary tangles, overview 2.7.11.26 ATP + tau-protein - 2.7.11.26 ATP + tau-protein ERK2 phosphorylates Thr-50, Thr-153, Thr-175, Thr-181, Thr-205, Thr-231, Ser-235, Ser-404, and Ser-422 in tau-protein 2.7.11.26 ATP + tau-protein isoform TTBK1 is the isoform responsible for tau phosphorylation at epitopes enriched in tauopathies such as serine 422 2.7.11.26 ATP + tau-protein isoform TTBK1 phosphorylates tau-protein at Ser198, Ser199, Ser202 and Ser422 2.7.11.26 ATP + tau-protein phosphorylation at Ser-422 2.7.11.26 ATP + tau-protein phosphorylation on Ser198, Ser199, Ser202, and Ser422 2.7.11.26 ATP + tau-protein tau tubulin kinase 2 phosphorylates tau-protein at Ser208 and Ser210 2.7.11.26 ATP + TDP-43 - 2.7.11.26 ATP + tubulin - 2.7.11.26 ATP + [amyloid precursor protein] phosphorylation of the intracellular domain Thr668 of APP by GSK-3beta 2.7.11.26 ATP + [tau-protein] - 2.7.11.26 ATP + [tau-protein] 14-3-3 connects glycogen synthase kinase-3 beta to tau within a brain microtubule-associated tau phosphorylation complex 2.7.11.26 ATP + [tau-protein] abnormal hyperphosphorylation of tau by PKA and GSK-3 is associated with Alzheimer's disease and other tauopaties leading to neuronal degeneration 2.7.11.26 ATP + [tau-protein] activity in organisms with mutated APP and tau, not in wild-type, overview 2.7.11.26 ATP + [tau-protein] cdk5 associated with p25 2.7.11.26 ATP + [tau-protein] cdk5 substrate in brain, cdk5 associated with p39, tau is a microtubule-associated and developmentally regulated protein involved in axonal development in neurons, tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules 2.7.11.26 ATP + [tau-protein] hyperphosphorylation of tau by CDK5 is involved in apoptosis and neurodegeneration in Alzheimer's disease, overview 2.7.11.26 ATP + [tau-protein] phosphorylation of tau, especially at the primed epitope T231 negatively regulates tau-microtubule interactions, different effects of phosphorylation on primed T231 and unprimed S396/S404 epitopes of tau, overview 2.7.11.26 ATP + [tau-protein] protein 14-3-3 mediates phosphorylation of microtubule-associated protein tau by serum- and glucocorticoid-induced protein kinase 1 SGK1, which forms an activated ternary complex with protein 14-3-3theta 2.7.11.26 ATP + [tau-protein] regulation, overview 2.7.11.26 ATP + [tau-protein] tau is microtubule-associated, phopshorylation at T231 by CDK5 causes its release into the cytoplasm 2.7.11.26 ATP + [tau-protein] tau is primarily found in neurons, regulation of tau phosphorylation by GSK3beta via interaction with FRAT-1 and FRAT-2, i.e. frequently rearranged in advanced T-cell lymphoma proteins 2.7.11.26 ATP + [tau-protein] tau phosphorylation by GSK-3beta is involved in development of neurodegenerative Alzheimer's disease, the tau phosphorylation activity by GSK-3beta is further increased by soluble toxic beta-amyloid oligomers, overview 2.7.11.26 ATP + [tau-protein] tau phosphorylation in vivo is stimulated by extracellular signal-regulated kinase Erk phosphorylation and apolipoprotein isozyme E4, to a lesser extent by isozyme apoE3, overview 2.7.11.26 ATP + [tau-protein] AMPK is one of the main tau kinase phosphorylating tau at the epitopes Ser262/356 and Thr231 at basal conditions in neurons 2.7.11.26 ATP + [tau-protein] phoshorylation at residues Ser404, Ser199, Ser202 and Thr231 2.7.11.26 ATP + [tau-protein] phosphorylation at Ser208 and Ser210 2.7.11.26 ATP + [tau-protein] phosphorylation of tau at various sites 2.7.11.26 ATP + [tau-protein] recombinant human tau protein expressed in transgenic mice 2.7.11.26 ATP + [tau-protein] tau isoforms in the human central nervous system and GSK-3 phosphorylation sites. Isozymes GSK-3alpha and GSK-3beta1/2 differentially phosphorylate tau, e.g. Ser396 in tau is phosphorylated by both splice variants, whereas Ser199 is a significant target of GSK-3beta1, but not of GSK-3beta2 activity 2.7.11.26 additional information - 2.7.11.26 additional information enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells 2.7.11.26 additional information possible role of the sgg protein in a signal transduction pathway necessary for intercellular communication at different stages of development 2.7.11.26 additional information implicated in cell-fate determination and differentiation, phosphorylates several regulatory proteins that are activated by dephosphorylation in response to hormones or growth factors 2.7.11.26 additional information enzyme of the lithium-sensitive wnt signaling pathway 2.7.11.26 additional information enzyme acts as a repressor of engrailed autoregulation 2.7.11.26 additional information enzyme forms part of the wingless signalling pathway. GSK-3beta activity is negatively regulated by phosphorylation on serine 9 and positively regulated by phosphorylation on tyrosine 216. Enzyme may also be regulated at the transcriptional level 2.7.11.26 additional information implicated in the hormonal control of several regulatory proteins including glycogen synthase and the transcription factor c-jun 2.7.11.26 additional information MDS1 is not essential during normal vegetative growth but appears to be required for meiosis 2.7.11.26 additional information enzyme regulates cell fate in Dictyostelium 2.7.11.26 additional information enzyme is involved in the induction of meiosis 2.7.11.26 additional information MCK1 encodes a positive regulator of meiosis and spore formation. MCK1 is required in vegetative cells for basal IME1 expression, it is also required for efficient ascus maturation. MCK1 plays a role in governing centromere function during vegetative growth as well as sporulation 2.7.11.26 additional information AtK-1 kinase is involved in reproduction-specific processes 2.7.11.26 additional information abnormal phosphorylation of tau in dividing cells leads to its accumulation in the cytosol as microtubule-free form, Cdk5 is involved in neurodegenerative mechanisms 2.7.11.26 additional information activation and deregulation of GSK-3, e.g. by wortmannin or GF-109203X, induces Alzheimer-like tau hyperphosphorylation in hippocampus, the hyperphosphorylated tau forms neurofibrillary tangle 2.7.11.26 additional information CDK5-dependent clustering of endoplasmic reticulum ER and mitochondria during ceramide-mediated neuronal death: neurotoxic calcium transfer from ER to mitochondria is regulated by cyclin-dependent kinase 5-dependent phosphorylation of tau, inhibition of the process leads to cell death 2.7.11.26 additional information glycogen synthase kinase-3beta also performs serine/threonine protein kinase reaction, EC 2.7.11.1, with other substrates than tau, e.g. it phosphorylates the glycogen synthase 2.7.11.26 additional information GSK-3 affects the tau-mRNA splicing of exon 10 via phosphorylation of the splicing factors of the serine/arginine-rich splicing factor SR family, e.g. SC35, leading to priming and dislocation of the splicing factor, aberrant tau splicing contributes to tauopathies including Alzheimer's disease, overview 2.7.11.26 additional information GSK3beta and PKA work coordinatedly on tau phosphorylation 2.7.11.26 additional information naturally occurring V717I mutation of the amyloid precursor protein APP in a CT100 fragment of mutants leads to augmented age-dependent tau phosphorylation, followed by increased activation status of mitogen-activated protein kinase family members, e.g. ERK1/2, p38, and c-Jun NH2-terminal kinase, compared to the wild-type organism, naturally occurring V337M mutation of tau protein of mutants leads to age-dependent memory deficits 2.7.11.26 additional information naturally occurring V717I mutation of the amyloid precursor protein APP in a CT100 fragment of organisms with Alzheimer's disease leads to augmented age-dependent tau phosphorylation, followed by increased activation status of mitogen-activated protein kinase family members, e.g. ERK1/2, p38, and c-Jun NH2-terminal kinase, compared to the wild-type organism, naturally occurring V337M mutation of tau protein of patients suffering from Alzheimer's disease leads to age-dependent memory deficits 2.7.11.26 additional information phosphorylated tau is important in cytoskeleton assembly 2.7.11.26 additional information protein 14-3-3 facilitates tau phosphorylation by SGK1 and regulates its subcellular localization in the nucleus or cytoplasm, overview 2.7.11.26 additional information rapid, reversible cold-water stress-induced hyperphosphorylation of tau S199, S202, T205, T231, and S235 in hippocampal and cerebral region of the brain, hyperphosphorylation of tau is associated to the Alzheimer's disease 2.7.11.26 additional information tau becomes a more favorable substrate for GSK-3 when it is prephosphorylated by PKA in rat brain, inhibition of tau hyperphosphorylation inhibits an associated loss in spatial memory 2.7.11.26 additional information the enzyme participates in Alzheimer's disease 2.7.11.26 additional information glycogen synthase kinase-3 isoforms have distinct substrate preference in the brain, overview 2.7.11.26 additional information glycogen synthase kinase-3 isoforms have distinct substrate preference in the brain. There are GSK3 substrates with preference for GSK3beta1 over GSK3beta2, and others that hold no distinction, suggesting different modes of interaction with GSK3, overview 2.7.11.26 additional information in addition to autophosphorylation, known phosphorylation substrates of TTBK2 include tau, tubulin, CEP164, CEP97, and TDP-43, a neurodegeneration-associated protein. The enzyme binds to CEP164, a centriolar protein, and EB1, a microtubule plus-end tracking protein