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Information on EC 2.7.11.26 - tau-protein kinase and Organism(s) Rattus norvegicus and UniProt Accession P18266
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2.7.11.26 tau-protein kinaseIUBMB Comments
Activated by tubulin. Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease.
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- 2.7.11.26
- obesity
- rapamycin
- metformin
- carboxylase
- mtor
- aicar
- peroxisome
- cardiac
- endothelial
-
proliferator-activated
- alzheimer
- adipose
- acetyl-coa
-
high-fat
- necrosis
- mapks
- adipocytes
- triglyceride
- agonist
- myocardial
- 3-kinase
- adiponectin
-
obese
- phosphatidylinositol
-
signal-regulated
-
neuroprotective
- cardiomyocytes
-
hyperphosphorylation
- sirt1
-
lipogenesis
-
diet-induced
- leptin
-
element-binding
- myotubes
-
antidiabetic
- carnitine
- steatosis
-
cardioprotective
- sirtuins
-
receptor-interacting
-
insulin-stimulated
-
rho-associated
-
hfd-induced
-
necroptosis
- ripk1
-
anti-obesity
-
monophosphate-activated
- srebp-1c
- coactivator-1
- ulk1
- drug development
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
amp-activated protein kinase, glycogen synthase kinase, protein kinase 1, gsk3b, extracellular-regulated kinase, gsk-3 beta, protein kinase-a, srpk2, gsk-3alpha, ttbk2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Gasket protein
-
-
-
-
glycogen synthase kinase
-
-
-
-
glycogen synthase kinase-3beta
-
-
GSK-3
GSK-3 alpha
-
-
-
-
GSK-3 beta
GSK-3beta
-
-
protein tau kinase
-
-
-
-
tau factor protein kinase (phosphorylating)
-
-
-
-
tau kinase
-
-
-
-
tau protein kinase
tau protein kinase I
-
-
-
-
additional information
GSK-3 beta
-
-
-
-
tau protein kinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [tau-protein] = ADP + O-phospho-[tau-protein]
GSK-3 and PKA catalyze tau phosphorylation in the brain, while GSK-3 performs phosphorylation of glycogen synthase, EC 2.7.11.1, and other proteins in different tissues, and PKA performs phosphorylation of other proteins in different tissues
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[tau-protein] O-phosphotransferase
Activated by tubulin. Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease.
CAS REGISTRY NUMBER
COMMENTARY
111694-09-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + protein PHF-1 (Ser396/404)
ADP + protein PHF-1 (Ser396/404) phosphate
-
-
-
?
ATP + H-Arg-Arg-Arg-Ala-Ala-Glu-Glu-Leu-Asp-Ser-Arg-Ala-Gly-pSer-Pro-Gln-Leu-OH
ADP + ?
-
-
-
-
?
ATP + tau-protein
ADP + O-phospho-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
-
-
?
glycogen synthase + ATP
phosphorylated glycogen synthase + ADP
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
phosphorylation of tau at various sites
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
phosphorylation at Ser198, Ser199, Ser202, Ser396, and Ser404
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
tau phosphorylation at GSK-3beta sensitive but AMPK insensitive residues Ser202/Thr205
-
-
?
glycogen synthase + ATP
phosphorylated glycogen synthase + ADP
-
-
-
?
glycogen synthase + ATP
phosphorylated glycogen synthase + ADP
-
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
microtubule-associated protein, enzyme can also phosphorylate human tau
-
?
ATP + protein tau
ADP + protein tau phosphate
-
microtubule-associated protein
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
abnormal hyperphosphorylation of tau by PKA and GSK-3 is associated with Alzheimer's disease and other tauopaties leading to neuronal degeneration
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
tau is microtubule-associated, phopshorylation at T231 by CDK5 causes its release into the cytoplasm
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
phosphorylation at T231, no activity with tau mutant T231A
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
phosphorylation by PKA at Ser214, and by GSK-3 at Ser404, Ser396, Ser198, Ser199, and Ser202
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
additional information
?
-
implicated in the hormonal control of several regulatory proteins including glycogen synthase and the transcription factor c-jun
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
does not phosphorylate tau at epitope Ser 262
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + tau-protein
ADP + O-phospho-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
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
phosphorylation of tau at various sites
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
microtubule-associated protein
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
abnormal hyperphosphorylation of tau by PKA and GSK-3 is associated with Alzheimer's disease and other tauopaties leading to neuronal degeneration
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
tau is microtubule-associated, phopshorylation at T231 by CDK5 causes its release into the cytoplasm
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
additional information
?
-
implicated in the hormonal control of several regulatory proteins including glycogen synthase and the transcription factor c-jun
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
additional information
?
-
enzyme is involved in the cellular response to insulin, the enzyme is highly phosphorylated on tyrosine and thus active in resting cells
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lithium
selective inhibition of GSK-3, blocks tau hyperphosphorylation either in cultured neurons or in rat brain
(Rp)-adenosine 3',5'-cyclic monophosphorothionate triethyl ammonium salt
-
inhibitor of PKA
3alpha,5alpha-tetrahydroprogesterone
-
decreases only expression of GSK-3 beta in the cerebellum but not in the hypothalamus
5alpha-dihydroprogesterone
-
decreases only expression of GSK-3 beta in the cerebellum but not in the hypothalamus
A-582941
-
attenuates beta-amyloid peptide 1-42-induced activation of GSK-3beta
alpha-bungarotoxin
-
attenuates beta-amyloid peptide 1-42-induced activation of GSK-3beta
ATP
-
strongly inhibited by elevated concentrations of ATP uncomplexed with magnesium
caffeic acid
-
0.02 mg/ml caffeic acid decreases the activating phosphorylation of GSK-3beta
CHIR98023
-
attenuates beta-amyloid peptide 1-42-induced activation of GSK-3beta
dantrolene
-
in the presence of dantrolene, GSK-3beta activation and tau phosphorylation are decreased
Insulin
-
insulin induces phosphorylation of the Ser9 residue, thereby inactivating GSK-3beta
-
methyllycaconitine
-
attenuates beta-amyloid peptide 1-42-induced activation of GSK-3beta
Nicotine
-
attenuates beta-amyloid peptide 1-42-induced activation of GSK-3beta
progesterone
-
decreases expression and phosphorylation of GSK-3 beta in the cerebellum but not in the hypothalamus, regulation of tau expression and phosphorylation by progesterone may contribute to the hormonal regulation of cerebellar function by the modification of neuronal cytoskeleton
Protein kinase C
-
protein kinase C inhibits GSK-3beta by phosphorylating its auto-inhibitory domain at Ser9
-
TDZD-8
-
selective GSK-3beta inhibitor, induces phosphorylation of the Ser9 residue, thereby inactivating GSK-3beta
LiCl
-
lithium is a weak inhibitor of GSK3beta, lithium dose-dependently inhibits GSK3beta through the phosphorylation of serine 9 residue
SB216763
-
potent and selective cell permeable ATP-competitive inhibitor of GSK3
additional information
GSK-3 is inactivated by phosphorylation of serine 9 in GSK-3beta and serine 21 in GSK-3alpha subunits by mainly Akt. Hyperglycemia induces strong activity of GSK-3 in rat brain
-
additional information
-
phosphorylation of GSK3beta at S9 inhibits the enzyme, the phosphorylation at Ser9 is inhibited by wortmannin or GF-109203X, this inhibition is eliminated by inhibition of GSK-3 by a different inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-amyloid peptide 1-42
-
0.01 mM, induces phosphorylation at Tyr216 activating GSK-3beta
-
p25
-
activator required for CDK5 activity, activation of CDK5 by p25 which is activated by cleavage of p35 to p25
-
tubulin
-
stimulates phosphorylation of tau under the condition of microtubile formation
-
additional information
GSK-3beta is activated by inhibition of both Wnt and PI3K/Akt signaling
-
additional information
-
not activated by cyclic nucleotides cAMP and cGMP, calmodulin or phospholipide
-
additional information
-
tau becomes a more favorable substrate for GSK-3 when it is prephosphorylated by PKA in rat brain
-
additional information
-
treatment of the hippocampus cells with phosphoinositol 3-kinase inhibitor wortmannin or protein kinase C inhibitor GF-109203X leads to tau hyperphosphorylation both at Ser396/404 and at Ser199/202, with both inhibitors acting synergistically to each other, resulting in Alzheimer's disease-like tau accumulation, overview, wortmannin or GF-109203X decrease the phosphorylation of GSK-3 at Ser9, inhibition of the GSK-3 eliminates the effects of wortmannin and GF-109203X leads to tau hyperphosphorylation both at Ser396/404 and at Ser199/202, with both inhibitors acting synergistically with each other, resulting in Alzheimer's disease-like tau accumulation, overview, wortmannin or GF-109203X
-
additional information
-
glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2-mediated proteolysis (dephosphorylation of Ser-9) in cardiomyoblasts MMP-2, GSK-3beta may be a target of matrix metalloproteinase-2 and its cleavage by matrix metalloproteinase-2 enhances its kinase activity, matrix metalloproteinase-2-mediated augmentation of GSK-3beta kinase activity may contribute to cardiac injury resulting from enhanced oxidative stress
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
when amyloid precursor protein is overexpressed, the GSK-3beta phosphorylated at Tyr216 level significantly increases in the nuclear fraction
additional information
-
CDK5-dependent clustering of endoplasmic reticulum ER and mitochondria and translocation to the centrosome during ceramide-mediated neuronal death
-
-
GSK-3beta phosphorylated at Tyr216 is mainly localized in cytoplasm
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
abnormal tau phosphorylation (p-tau) occurs after hypoxic damage to the brain associated with traumatic brain injury and stroke
physiological function
malfunction
-
inhibition of GSK-3beta mediates Nrf2 activation by the M1 receptor
physiological function
physiological function
glycogen synthase kinase-3 (GSK-3beta) and protein phosphatase 2A (PP2A) are thought to control the levels of tau phosphorylation. No alteration in the activities of GSK-3beta and PP2A during episodes of ischaemia of up to 8 min and reperfusion of up to 2 h, and 4 weeks recovery. Tau dephosphorylation following ischaemia is not dependent on GSK-3beta or PP2A activity, but is associated with AMPK dephosphorylation
physiological function
glycogen synthase kinase-3 plays an important role in the pathogenesis of Diabetes mellitus and Alzheimer's disease. Diabetic rats display an increased GSK-3 activity, and decreased activity and expression of Akt. And Abeta40 and Abeta42 are overproduced and the microtubule-associated protein tau is hyperphosphorylated in the hippocampus. Selective inhibition of GSK-3 attenuates the conditions of Abeta overproduction and tau hyperphosphorylation. GSK-3 regulates both the production of Amyloidbeta and the phosphorylation of tau in rat brain and may therefore contribute to Diabetes mellitus caused Alzheimer disease-like neurological defects. Hyperglycemia induces strong activity of GSK-3 and lowers activity of Akt in rat brain. The production of Abeta40 and Abeta42 is increased significantly while activation of GSK-3 and inhibition of Akt are induced in Diabetes mellitus
physiological function
-
GSK-3beta is a multifunctional Ser/Thr kinase that plays important roles in necrosis and apoptosis of cardiomyocytes
physiological function
-
GSK3beta regulates both tau phosphorylation and total tau levels through protein phosphatase-2A
physiological function
-
protein tau phosphorylation plays an essential role in adult hippocampal neurogenesis and GSK-3 facilitates neurogenesis only in the presence of tau proteins, tau hyperphosphorylation induced by activating GSK-3 promotes neurogenesis
physiological function
-
the neuron-specific isoform GSK-3beta2 is required for axon growth by phosphorylating microtubule-associated proteins including protein tau
physiological function
-
ERK2 dysregulation in Alzheimer's disease can lead to abnormal phosphorylation of Tau resulting in the pathology of the disease
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GSK3B_RAT
420
0
46742
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
GSK-3 is inactivated by phosphorylation of serine 9 in GSK-3beta and serine 21 in GSK-3alpha subunits. Akt appears to be the predominant kinase mediating this phosphorylation of GSK-3
phosphoprotein
phosphoprotein
-
phosphorylation of GSK3beta by a different protein kinase, e.g. phosphoinositol 3-kinase or protein kinase C, at Ser9 inhibits the enzyme
phosphoprotein
-
activity of GSK3beta is regulated through phosphorylation on serine-9 (inhibitory) and tyrosine-216 residues (stimulatory)
phosphoprotein
-
phosphorylation of GSK-3beta at Ser9 reduces activity of this kinase
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of dominant negative EGFP-tagged CDK5 and p25 in PC12 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
administration of insulin or TDZD-8 to diabetic rats does not modify the total GSK-3beta mRNA levels
-
after lactacystin treatment, the total level of GSK-3beta does not change while the Ser-9-phosphorylated GSK-3beta (inactive form) decreases, especially at 72 h
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
brain pathology in investigation of Alzheimers's disease, human tau phosphorylated by the kinase carries an epitope of the paired helical filaments that accumulate in the brain
medicine
-
PKA and GSK-3 are targets for the therapeutic treatment of Alzheimer's disease and other tauopathies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lepage, T.; Gache, C.
Early expression of a collagenase-like hatching enzyme gene in the sea urchin embryo
EMBO J.
9
3003-3012
1990
Rattus norvegicus (P18265)
Hughes, K.; Nikolakaki, E.; Plyte, S.E.; Totty, N.F.; Woodgett, J.R.
Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
EMBO J.
12
803-808
1993
Rattus norvegicus (P18265), Rattus norvegicus (P18266), Drosophila melanogaster (P18431), Drosophila melanogaster
Ishiguro, K.; Shiratsuchi, A.; Sato, S.; Omori, A.; Arioka, M.; Kobayashi, S.; Uchida, T.; Imahori, K.
Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filaments
FEBS Lett.
325
167-172
1993
Rattus norvegicus (P18266)
Woodgett, J.R.
Molecular cloning and expression of glycogen synthase kinase-3/factor A
EMBO J.
9
2431-2438
1990
Rattus norvegicus (P18266)
Ishiguro, K.; Ihara, Y.; Uchida, T.; Imahori, K.
A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau
J. Biochem.
104
319-321
1988
Rattus norvegicus
Bush, M.L.; Miyashiro, J.S.; Ingram, V.M.
Activation of a neurofilament kinase, a tau kinase, and a tau phosphatase by decreased ATP levels in nerve growth factor-differentiated PC-12 cells
Proc. Natl. Acad. Sci. USA
92
1861-1865
1995
Rattus norvegicus
Takahashi, M.; Tomizawa, K.; Ishiguro, K.; Takamatsu, M.; Fujita, S.C.; Imahori, K.
Involvement of tau protein kinase I in paired helical filament-like phosphorylation of the juvenile tau in rat brain
J. Neurochem.
64
1759-1768
1995
Rattus norvegicus, Rattus norvegicus Wistar
Hoshi, M.; Takashima, A.; Noguchi, K.; Murayama, M.; Sato, M.; Kondo, S.; Saitoh, Y.; Ishiguro, K.; Hoshino, T.; Imahori, K.
Regulation of mitochondrial pyruvate dehydrogenase activity by tau protein kinase I/glycogen synthase kinase 3beta in brain
Proc. Natl. Acad. Sci. USA
93
2719-2723
1996
Homo sapiens, Rattus norvegicus
Imahori, K.; Uchida, T.
Physiology and pathology of tau protein kinases in relation to Alzheimer's disease
J. Biochem.
121
179-188
1997
Homo sapiens, Rattus norvegicus
Alvarez, A.; Toro, R.; Caceres, A.; Maccioni, R.B.
Inhibition of tau phosphorylating protein kinase cdk5 prevents beta-amyloid-induced neuronal death
FEBS Lett.
459
421-426
1999
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Tomizawa, K.; Omori, A.; Ohtake, A.; Sato, K.; Takahashi, M.
tau-Tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites found in paired helical filament-tau
FEBS Lett.
492
221-227
2001
Bos taurus, Mus musculus, Mus musculus (Q3UVR3), Rattus norvegicus, Rattus norvegicus Wistar
Mukai, F.; Ishiguro, K.; Sano, Y.; Fujita, S.C.
Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3beta
J. Neurochem.
81
1073-1083
2002
Homo sapiens, Mus musculus, Rattus norvegicus
Liu, S.J.; Zhang, J.Y.; Li, H.L.; Fang, Z.Y.; Wang, Q.; Deng, H.M.; Gong, C.X.; Grundke-Iqbal, I.; Iqbal, K.; Wang, J.Z.
Tau becomes a more favorable substrate for GSK-3 when it is prephosphorylated by PKA in rat brain
J. Biol. Chem.
279
50078-50088
2004
Rattus norvegicus
Li, X.; Lu, F.; Tian, Q.; Yang, Y.; Wang, Q.; Wang, J.Z.
Activation of glycogen synthase kinase-3 induces Alzheimer-like tau hyperphosphorylation in rat hippocampus slices in culture
J. Neural Transm.
113
93-102
2006
Rattus norvegicus
Darios, F.; Muriel, M.P.; Khondiker, M.E.; Brice, A.; Ruberg, M.
Neurotoxic calcium transfer from endoplasmic reticulum to mitochondria is regulated by cyclin-dependent kinase 5-dependent phosphorylation of tau
J. Neurosci.
25
4159-4168
2005
Rattus norvegicus
Guerra-Araiza, C.; Amorim, M.A.; Camacho-Arroyo, I.; Garcia-Segura, L.M.
Effects of progesterone and its reduced metabolites, dihydroprogesterone and tetrahydroprogesterone, on the expression and phosphorylation of glycogen synthase kinase-3 and the microtubule-associated protein tau in the rat cerebellum
Dev. Neurobiol.
67
510-520
2007
Rattus norvegicus
Hu, M.; Waring, J.F.; Gopalakrishnan, M.; Li, J.
Role of GSK-3beta activation and alpha7 nAChRs in Abeta(1-42)-induced tau phosphorylation in PC12 cells
J. Neurochem.
106
1371-1377
2008
Rattus norvegicus
Resende, R.; Ferreiro, E.; Pereira, C.; Oliveira, C.R.
ER stress is involved in Abeta-induced GSK-3beta activation and tau phosphorylation
J. Neurosci. Res.
86
2091-2099
2008
Rattus norvegicus
Mercado-Gomez, O.; Hernandez-Fonseca, K.; Villavicencio-Queijeiro, A.; Massieu, L.; Chimal-Monroy, J.; Arias, C.
Inhibition of Wnt and PI3K signaling modulates GSK-3beta activity and induces morphological changes in cortical neurons: role of tau phosphorylation
Neurochem. Res.
33
1599-1609
2008
Rattus norvegicus (P18266)
Martin, L.; Magnaudeix, A.; Esclaire, F.; Yardin, C.; Terro, F.
Inhibition of glycogen synthase kinase-3beta downregulates total tau proteins in cultured neurons and its reversal by the blockade of protein phosphatase-2A
Brain Res.
1252
66-75
2009
Rattus norvegicus
Kandasamy, A.D.; Schulz, R.
Glycogen synthase kinase-3beta is activated by matrix metalloproteinase-2 mediated proteolysis in cardiomyoblasts
Cardiovasc. Res.
83
698-706
2009
Rattus norvegicus
Miura, T.; Miki, T.
GSK-3beta, a therapeutic target for cardiomyocyte protection
Circ. J.
73
1184-1192
2009
Rattus norvegicus
Collino, M.; Aragno, M.; Castiglia, S.; Tomasinelli, C.; Thiemermann, C.; Boccuzzi, G.; Fantozzi, R.
Insulin reduces cerebral ischemia/reperfusion injury in the hippocampus of diabetic rats: a role for glycogen synthase kinase-3beta
Diabetes
58
235-242
2009
Rattus norvegicus
Hong, X.P.; Peng, C.X.; Wei, W.; Tian, Q.; Liu, Y.H.; Yao, X.Q.; Zhang, Y.; Cao, F.Y.; Wang, Q.; Wang, J.Z.
Essential role of tau phosphorylation in adult hippocampal neurogenesis
Hippocampus
20
1339-1349
2010
Rattus norvegicus
Gao, H.K.; Yin, Z.; Zhang, R.Q.; Zhang, J.; Gao, F.; Wang, H.C.
GSK-3beta inhibitor modulates TLR2/NF-kappaB signaling following myocardial ischemia-reperfusion
Inflamm. Res.
58
377-383
2009
Rattus norvegicus
Yotsumoto, K.; Saito, T.; Asada, A.; Oikawa, T.; Kimura, T.; Uchida, C.; Ishiguro, K.; Uchida, T.; Hasegawa, M.; Hisanaga, S.
Effect of Pin1 or microtubule binding on dephosphorylation of FTDP-17 mutant Tau
J. Biol. Chem.
284
16840-16847
2009
Rattus norvegicus
Burgos-Ramos, E.; Martos-Moreno, G.A.; Lopez, M.G.; Herranz, R.; Aguado-Llera, D.; Egea, J.; Frechilla, D.; Cenarruzabeitia, E.; Leon, R.; Arilla-Ferreiro, E.; Argente, J.; Barrios, V.
The N-terminal tripeptide of insulin-like growth factor-I protects against beta-amyloid-induced somatostatin depletion by calcium and glycogen synthase kinase 3beta modulation
J. Neurochem.
109
360-370
2009
Rattus norvegicus
Espada, S.; Rojo, A.I.; Salinas, M.; Cuadrado, A.
The muscarinic M1 receptor activates Nrf2 through a signaling cascade that involves protein kinase C and inhibition of GSK-3beta: connecting neurotransmission with neuroprotection
J. Neurochem.
110
1107-1119
2009
Rattus norvegicus
Sul, D.; Kim, H.S.; Lee, D.; Joo, S.S.; Hwang, K.W.; Park, S.Y.
Protective effect of caffeic acid against beta-amyloid-induced neurotoxicity by the inhibition of calcium influx and tau phosphorylation
Life Sci.
84
257-262
2009
Rattus norvegicus
Liu, Y.H.; Wei, W.; Yin, J.; Liu, G.P.; Wang, Q.; Cao, F.Y.; Wang, J.Z.
Proteasome inhibition increases tau accumulation independent of phosphorylation
Neurobiol. Aging
30
1949-1961
2009
Rattus norvegicus
Pajak, B.; Songin, M.; Strosznajder, J.B.; Gajkowska, B.
Alzheimers disease genetic mutation evokes ultrastructural alterations: correlation to an intracellular Abeta deposition and the level of GSK-3beta-P(Y216) phosphorylated form
Neurotoxicology
30
581-588
2009
Rattus norvegicus
Majd, S.; Power, J.H.; Koblar, S.A.; Grantham, H.J.
Early glycogen synthase kinase-3beta and protein phosphatase 2A independent tau dephosphorylation during global brain ischaemia and reperfusion following cardiac arrest and the role of the adenosine monophosphate kinase pathway
Eur. J. Neurosci.
44
1987-1997
2016
Rattus norvegicus (P18266), Rattus norvegicus Sprague-Dawley (P18266)
Qu, Z.S.; Li, L.; Sun, X.J.; Zhao, Y.W.; Zhang, J.; Geng, Z.; Fu, J.L.; Ren, Q.G.
Glycogen synthase kinase-3 regulates production of amyloid-beta peptides and tau phosphorylation in diabetic rat brain
ScientificWorldJournal
2014
878123
2014
Rattus norvegicus (P18266)
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