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Validated All-in-One™ qPCR Primer for GSK3A(NM_019884.2) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
Glycogen synthase kinase 3-alpha (GSK3A; EC {2.7.1.37}) is a multifunctional protein serine kinase, homologous to Drosophila 'shaggy' (zeste-white3) and implicated in the control of several regulatory proteins including glycogen synthase (see GYS1, {138570}) and transcription factors (e.g., JUN, {165160}). It also plays a role in the WNT ({164820}) and PI3K (see PIK3CG, {601232}) signaling pathways (see review by {1:Ali et al. (2001)}).[supplied by OMIM].
Gene References into function
- improves insulin action and glucose metabolism in skeletal muscle
- Paper shows that GSK-3 isoforms are not functionally equivalent in regulating the production of Abeta peptides. siRNA used to knockdown endogenous GSK-3 isoforms in cultured cells.
- GSK3alpha is a potential regulator of platelet function
- Data show that myotubes defective in glycogen synthase (GS) activity express insulin-responsive glycogen synthase kinase-3alpha, suggesting that failure of insulin to decrease GS phosphorylation involves abnormal activity of another kinase or phosphatase
- Data show that the activity of glycogen synthase kinase-3 (GSK-3) is necessary for the maintenance of the epithelial architecture, and that GSK-3 inhibition stimulates the transcription of Snail
- The results demonstrate that the control of MCL-1 stability by GSK-3 is an important mechanism for the regulation of apoptosis by growth factors, PI3K, and AKT.
- GSK3 alters phosphorylation of CRMP-1, -2, and -4 isoforms
- there is tissue specificity for the regulation of GSK-3 in humans; in skeletal muscle GSK-3 plays a role in control of metabolism and insulin action, whereas the function in adipose tissue is less clear
- Induction of keratinocyte migration is conveyed through EGFR, promoted by endogenous HB-EGF and requires GSK-3alpha activity.
- analysis of critical variations in the function and regulation of GSK-3alpha and GSK-3beta
- These results suggest i) an essential role of PI3K/Akt/GSK-3alpha/beta signaling for a successful replication of VZV and ii) a key function of VZV kinases pORFs 47 and 66 to activate this pathway.
- NT uses PKC-dependent pathways to modulate GSK-3, which may play a role in the NT regulation of intestinal cell growth
- These results indicate that the protein phosphatase-1/inhibitor-2 complex differentially regulates GSK3 dephosphorylation induced by KCl and that GSK3 activity regulates SERCA2 levels.
- S6K1 regulates GSK3 under conditions of mTOR-dependent feedback inhibition of Akt
- Glycogen synthase kinase 3alpha (GSK-3alpha) is identified as a partner for Cdc42 GTPase-activating protein (CdGAP).
- direct regulation of hypoxia-inducible factor 1 alpha subunit stability by GSK-3 may influence physiological processes or pathophysiological situations such as metabolic diseases or tumors
- Reduction of GSK3alpha expression results in improvements in insulin action and elevation of GSK3alpha in human skeletal muscle cells can induce insulin resistance for several responses
- GSK-3 is required for E2-induced ERalpha phosphorylation at Ser-118 and full transcriptional activity of the receptor upon E2 stimulation.
- Maf-transforming activity is controlled by GSK-3-dependent phosphorylation and that phosphorylation by GSK-3 can increase the oncogenic activity of a protein.
- Activin A may mediate ovarian oncogenesis by activating Akt and repressing GSK to stimulate cellular proliferation.
- inhibition of glycogen synthase kinase-3 in androgen-responsive prostate cancer cell lines may reduce AR transcriptional activity and AR protein levels
- GSK-3 and IKK as potential therapeutic targets for pancreatic cancer.
- This review concentrates on the role of protein kinase glycogen synthase kinase 3 in the different types of Alzheimers' disease.
- The authors found that threonine 10 of H1.5 can be phosphorylated by glycogen synthase kinase-3 in vitro
- Results describe a novel function of chaperonin 10 as a general differentiation factor, not limited to erythroid cells, and show how this biological effect is mediated by GSK-3alpha/beta.
