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GSK3A glycogen synthase kinase 3 alpha

glycogen synthase kinase 3 alpha
Top mentioned proteins: Akt, p70, CAN, MAPK, ERK
Papers on glycogen synthase kinase 3 alpha
Expression and inactivation of glycogen synthase kinase 3 alpha/ beta and their association with the expression of cyclin D1 and p53 in oral squamous cell carcinoma progression.
Rana et al., Rānchī, India. In Mol Cancer, 2014
BACKGROUND: The study aims to evaluate the expression and activity of glycogen synthase kinase 3 isoforms α/β (GSK3α/β) and to assess their oncogenic potential through a correlation with the expression of cyclin D1 and p53 in oral cancer.
Identification of the couple GSK3α/c-Myc as a new regulator of hexokinase II in benzo[a]pyrene-induced apoptosis.
Lagadic-Gossmann et al., Rennes, France. In Toxicol In Vitro, 2012
We show that while glycogen synthase kinase 3 beta (GSK3β) regulated the expression of HKII at the transcriptional level, glycogen synthase kinase 3 alpha (GSK3α) was involved in B[a]P-induced apoptosis via a decrease in c-Myc expression.
Inhibition of GSK3 by lithium, from single molecules to signaling networks.
Beaulieu et al., Québec, Canada. In Front Mol Neurosci, 2012
Among several targets, lithium has been shown to directly inhibit glycogen synthase kinase 3 alpha and beta (GSK3α and GSK3β).
Identification and regulation of glycogen synthase kinase-3 during bovine embryo development.
Lonergan et al., Dublin, Ireland. In Reproduction, 2010
GSK3A serine phosphorylation was positively correlated with embryo development
mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and regulates mTORC2 signaling.
Roux et al., Montréal, Canada. In Mol Cell Biol, 2010
In addition, phosphorylation of the Akt substrates FoxO1/3a and glycogen synthase kinase 3 alpha/beta (GSK3 alpha/beta) was found to be increased in these cells, indicating that S6K1-mediated phosphorylation of Rictor inhibits mTORC2 and Akt signaling.
Nav1.7 sodium channel-induced Ca2+ influx decreases tau phosphorylation via glycogen synthase kinase-3beta in adrenal chromaffin cells.
Wada et al., Miyazaki, Japan. In Neurochem Int, 2009
signal pathways converged on inhibitory phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation
Differential detection of phosphorylated glycogen synthase kinase 3 alpha and beta depending on blocking conditions.
Pillay et al., Nottingham, United Kingdom. In Anal Biochem, 2008
It is generally recommended that immunoblots using phosphospecific antibodies be performed using bovine serum albumin (BSA) instead of milk.
A phosphosite screen identifies autocrine TGF-beta-driven activation of protein kinase R as a survival-limiting factor for eosinophils.
Alam et al., Denver, United States. In J Immunol, 2008
Both agents inhibited S6 kinase, protein kinase Cepsilon, and glycogen synthase kinase 3 alpha and beta.
Leptin, skeletal muscle lipids, and lipid-induced insulin resistance.
O'Doherty et al., Pittsburgh, United States. In Am J Physiol Regul Integr Comp Physiol, 2007
Compared with controls (CONT), HL increased insulin sensitivity, as assessed by hyperinsulinemic-euglycemic clamp ( approximately 15%), and increased SkM Akt ( approximately 30%) and glycogen synthase kinase 3 alpha ( approximately 52%) phosphorylation.
Key role of the p110delta isoform of PI3K in B-cell antigen and IL-4 receptor signaling: comparative analysis of genetic and pharmacologic interference with p110delta function in B cells.
Vanhaesebroeck et al., London, United Kingdom. In Blood, 2006
p110delta activity is indispensable for BCR-induced DNA synthesis and phosphorylation of Akt/protein kinase B (PKB), forkhead transcription factor/forkhead box O3a (FOXO3a), and p70 S6 kinase (p70 S6K), with modest effects on the phosphorylation of glycogen synthase kinase 3 alpha/beta (GSK3alpha/beta) and extracellular signal-regulated kinase (Erk).
Protein kinase and protein phosphatase expression in amyotrophic lateral sclerosis spinal cord.
Pelech et al., Canada. In J Neurochem, 2003
In both the cytosolic (C) and particulate (P) fractions of spinal cord from ALS patients as compared with controls, there were increased levels of calcium/calmodulin-dependent protein kinase kinase (CaMKK; C = 120% increase/P = 580% increase;% change, compared with control), extracellular regulated kinase 2 (ERK2; C = 120% increase/P = 170% increase), G protein-coupled receptor kinase 2 (GRK2; C = 140% increase/P = 140% increase), phospho-Y279/216 glycogen synthase kinase 3 alpha/beta (GSK3alpha/beta; C = 90% increase/P = 220% increase), protein kinase B alpha (PKBalpha; C = 360% increase/P = 200% increase), phospho-T638 PKCalpha/beta (C = 630% increase/P = 170% increase), cGMP-dependent protein kinase (PKG; C = 100% increase/P = 75% increase), phospho-T451 dsRNA-dependent protein kinase (PKR; C = 2600% increase/P = 3330% increase), ribosomal S6 kinase 1 (RSK1; C = 750% increase/P = 630% increase), phospho-T389 p70 S6 kinase (S6K; C = 1000% increase/P = 460% increase), and protein-tyrosine phosphatase 1 delta (PTP1delta; C = 43% increase/P = 70% increase).
Insulin receptor substrate-2 phosphorylation is necessary for protein kinase C zeta activation by insulin in L6hIR cells.
Beguinot et al., Napoli, Italy. In J Biol Chem, 2001
The impairment of GS activation was paralleled by a similarly sized inhibition of glycogen synthase kinase 3 alpha (GSK3 alpha) and GSK3 beta inactivation by insulin with no change in protein phosphatase 1 activity.
Transcriptional activity of heat shock factor 1 at 37 degrees C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Calpha and Czeta.
Calderwood et al., Boston, United States. In J Biol Chem, 1998
In vivo expression of glycogen synthase kinase 3 alpha or beta thus represses HSF1 through phosphorylation of serine 303.
Insulin-stimulated glycogen synthesis in cultured hepatoma cells: differential effects of inhibitors of insulin signaling molecules.
Scalia et al., Los Angeles, United States. In J Recept Signal Transduct Res, 1998
In these cells, insulin at 100 nM decreased glycogen synthase kinase 3 alpha (GSK3 alpha) activity by 30-35%.
Protein kinase FA/glycogen synthase kinase 3 alpha predominantly phosphorylates the in vivo sites of Ser502, Ser506, Ser603, and Ser666 in neurofilament.
Huang et al., Huazhou, China. In J Neurochem, 1995
In this report, the phosphorylation sites of neurofilament protein of medium molecular mass (NF-M) by protein kinase FA/glycogen synthase kinase 3 alpha (kinase FA/GSK-3 alpha) were determined by two-dimensional electrophoresis/TLC, phosphoamino acid analysis, HPLC, Edman degradation, and peptide sequencing.
Dephosphorylation of abnormal sites of tau factor by protein phosphatases and its implication for Alzheimer's disease.
Miyamoto et al., Kumamoto, Japan. In Neurochem Int, 1995
On the other hand, tau factor phosphorylated by glycogen synthase kinase 3 alpha was dephosphorylated by the catalytic subunit of protein phosphatases 2A as well as the holoenzyme of protein phosphatase 2A and calcineurin.
Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis.
Hann et al., Nashville, United States. In Mol Cell Biol, 1994
Hierarchical phosphorylation of c-Myc is also observed in vitro with a specific glycogen synthase kinase 3 alpha, unlike the promiscuous phosphorylation observed with other glycogen synthase kinase 3 alpha and 3 beta preparations.
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