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Gene Review

GSK3B  -  glycogen synthase kinase 3 beta

Homo sapiens

Synonyms: GSK-3 beta, Glycogen synthase kinase-3 beta, Serine/threonine-protein kinase GSK3B
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Disease relevance of GSK3B


Psychiatry related information on GSK3B


High impact information on GSK3B


Chemical compound and disease context of GSK3B


Biological context of GSK3B

  • We identified two functional single nucleotide polymorphisms in the glycogen synthase kinase-3beta gene (GSK3B) [1].
  • Ours results suggest GSK3B polymorphisms alter transcription and splicing and interact with Tau haplotypes to modify disease risk in PD [1].
  • The T allele is associated with altered splicing in lymphocytes and increased levels of GSK3B transcripts that lack exons 9 and 11 (GSKDeltaexon9+11) [1].
  • Canonical WNT signals are transduced through Frizzled receptor and LRP5/6 coreceptor to downregulate GSK3beta (GSK3B) activity not depending on Ser 9 phosphorylation [17].
  • However, it has not been reported the association analysis between GSK3beta gene (GSK3B) and Japanese schizophrenia based on linkage disequilibrium (LD) [18].

Anatomical context of GSK3B


Associations of GSK3B with chemical compounds


Physical interactions of GSK3B

  • In the present report, we have demonstrated that HdynIV interacts with the Gsk-3 beta through its carboxyl-terminal region, implying than HdynIV may also be involved in cell signaling [23].
  • The androgen receptor hinge and ligand-binding domains were important for both the phosphorylation and the inhibition of transcriptional activity of the receptor by glycogen synthase kinase-3 beta [21].
  • GSK3 beta binds to presenilin 1 and plays a role in wnt and insulin signalling cascades, both of which have been proposed to be linked to AD [6].
  • The inhibitory regulation of CREB DNA binding activity by GSK3 beta also was evident in differentiated SH-SY5Y cells, indicating that this regulatory interaction is maintained in non-proliferating cells [13].
  • Coimmunoprecipitation experiments show that full-length Notch2 binds more efficiently than intracellular Notch2 to GSK-3 beta [26].

Enzymatic interactions of GSK3B


Regulatory relationships of GSK3B


Other interactions of GSK3B


Analytical, diagnostic and therapeutic context of GSK3B


  1. GSK3B polymorphisms alter transcription and splicing in Parkinson's disease. Kwok, J.B., Hallupp, M., Loy, C.T., Chan, D.K., Woo, J., Mellick, G.D., Buchanan, D.D., Silburn, P.A., Halliday, G.M., Schofield, P.R. Ann. Neurol. (2005) [Pubmed]
  2. Proapoptotic stimuli induce nuclear accumulation of glycogen synthase kinase-3 beta. Bijur, G.N., Jope, R.S. J. Biol. Chem. (2001) [Pubmed]
  3. Suppression of androgen receptor-mediated transactivation and cell growth by the glycogen synthase kinase 3 beta in prostate cells. Wang, L., Lin, H.K., Hu, Y.C., Xie, S., Yang, L., Chang, C. J. Biol. Chem. (2004) [Pubmed]
  4. The GSK3 beta signaling cascade and neurodegenerative disease. Kaytor, M.D., Orr, H.T. Curr. Opin. Neurobiol. (2002) [Pubmed]
  5. Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. Wang, Q.M., Fiol, C.J., DePaoli-Roach, A.A., Roach, P.J. J. Biol. Chem. (1994) [Pubmed]
  6. Identification of sequence variants and analysis of the role of the glycogen synthase kinase 3 beta gene and promoter in late onset Alzheimer's disease. Russ, C., Lovestone, S., Powell, J.F. Mol. Psychiatry (2001) [Pubmed]
  7. A single nucleotide polymorphism in glycogen synthase kinase 3-beta promoter gene influences onset of illness in patients affected by bipolar disorder. Benedetti, F., Bernasconi, A., Lorenzi, C., Pontiggia, A., Serretti, A., Colombo, C., Smeraldi, E. Neurosci. Lett. (2004) [Pubmed]
  8. Long-term response to lithium salts in bipolar illness is influenced by the glycogen synthase kinase 3-beta -50 T/C SNP. Benedetti, F., Serretti, A., Pontiggia, A., Bernasconi, A., Lorenzi, C., Colombo, C., Smeraldi, E. Neurosci. Lett. (2005) [Pubmed]
  9. Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Dajani, R., Fraser, E., Roe, S.M., Young, N., Good, V., Dale, T.C., Pearl, L.H. Cell (2001) [Pubmed]
  10. Activation of the Wnt signaling pathway in chronic lymphocytic leukemia. Lu, D., Zhao, Y., Tawatao, R., Cottam, H.B., Sen, M., Leoni, L.M., Kipps, T.J., Corr, M., Carson, D.A. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  11. WNT7a induces E-cadherin in lung cancer cells. Ohira, T., Gemmill, R.M., Ferguson, K., Kusy, S., Roche, J., Brambilla, E., Zeng, C., Baron, A., Bemis, L., Erickson, P., Wilder, E., Rustgi, A., Kitajewski, J., Gabrielson, E., Bremnes, R., Franklin, W., Drabkin, H.A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  12. Testosterone prevents the heat shock-induced overactivation of glycogen synthase kinase-3 beta but not of cyclin-dependent kinase 5 and c-Jun NH2-terminal kinase and concomitantly abolishes hyperphosphorylation of tau: implications for Alzheimer's disease. Papasozomenos, S.C.h., Shanavas, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  13. CREB DNA binding activity is inhibited by glycogen synthase kinase-3 beta and facilitated by lithium. Grimes, C.A., Jope, R.S. J. Neurochem. (2001) [Pubmed]
  14. Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta. Aoki, M., Yokota, T., Sugiura, I., Sasaki, C., Hasegawa, T., Okumura, C., Ishiguro, K., Kohno, T., Sugio, S., Matsuzaki, T. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
  15. Immunocytochemistry of tau phosphoserine 413 and tau protein kinase I in Alzheimer pathology. Shiurba, R.A., Ishiguro, K., Takahashi, M., Sato, K., Spooner, E.T., Mercken, M., Yoshida, R., Wheelock, T.R., Yanagawa, H., Imahori, K., Nixon, R.A. Brain Res. (1996) [Pubmed]
  16. Role of glycogen synthase kinase 3 beta (GSK3beta) in mediating the cytotoxic effects of the histone deacetylase inhibitor trichostatin A (TSA) in MCF-7 breast cancer cells. Alao, J.P., Stavropoulou, A.V., Lam, E.W., Coombes, R.C. Mol. Cancer (2006) [Pubmed]
  17. Cross-talk of WNT and FGF Signaling Pathways at GSK3beta to Regulate beta-Catenin and SNAIL Signaling Cascades. Katoh, M., Katoh, M. Cancer Biol. Ther. (2006) [Pubmed]
  18. No association of GSK3beta gene (GSK3B) with Japanese schizophrenia. Ikeda, M., Iwata, N., Suzuki, T., Kitajima, T., Yamanouchi, Y., Kinoshita, Y., Ozaki, N. Am. J. Med. Genet. B Neuropsychiatr. Genet. (2005) [Pubmed]
  19. Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK II. Yamaguchi, H., Ishiguro, K., Uchida, T., Takashima, A., Lemere, C.A., Imahori, K. Acta Neuropathol. (1996) [Pubmed]
  20. Convergence of genes implicated in Alzheimer's disease on the cerebral cholesterol shuttle: APP, cholesterol, lipoproteins, and atherosclerosis. Carter, C.J. Neurochem. Int. (2007) [Pubmed]
  21. Glycogen synthase kinase-3 beta is involved in the phosphorylation and suppression of androgen receptor activity. Salas, T.R., Kim, J., Vakar-Lopez, F., Sabichi, A.L., Troncoso, P., Jenster, G., Kikuchi, A., Chen, S.Y., Shemshedini, L., Suraokar, M., Logothetis, C.J., DiGiovanni, J., Lippman, S.M., Menter, D.G. J. Biol. Chem. (2004) [Pubmed]
  22. Endogenous IGF-I protects human intestinal smooth muscle cells from apoptosis by regulation of GSK-3 beta activity. Kuemmerle, J.F. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  23. Human dynamin-like protein interacts with the glycogen synthase kinase 3beta. Hong, Y.R., Chen, C.H., Cheng, D.S., Howng, S.L., Chow, C.C. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  24. Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A. Fang, X., Yu, S.X., Lu, Y., Bast, R.C., Woodgett, J.R., Mills, G.B. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  25. Differential regulation of glycogen synthase kinase-3 beta by protein kinase C isotypes. Goode, N., Hughes, K., Woodgett, J.R., Parker, P.J. J. Biol. Chem. (1992) [Pubmed]
  26. Phosphorylation by glycogen synthase kinase-3 beta down-regulates Notch activity, a link for Notch and Wnt pathways. Espinosa, L., Inglés-Esteve, J., Aguilera, C., Bigas, A. J. Biol. Chem. (2003) [Pubmed]
  27. FRAT-2 preferentially increases glycogen synthase kinase 3 beta-mediated phosphorylation of primed sites, which results in enhanced tau phosphorylation. Stoothoff, W.H., Cho, J.H., McDonald, R.P., Johnson, G.V. J. Biol. Chem. (2005) [Pubmed]
  28. Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation. Zumbrunn, J., Kinoshita, K., Hyman, A.A., Näthke, I.S. Curr. Biol. (2001) [Pubmed]
  29. Mutational analysis of the APC/beta-catenin/Tcf pathway in colorectal cancer. Sparks, A.B., Morin, P.J., Vogelstein, B., Kinzler, K.W. Cancer Res. (1998) [Pubmed]
  30. Adenomatous polyposis coli (APC)-independent regulation of beta-catenin degradation via a retinoid X receptor-mediated pathway. Xiao, J.H., Ghosn, C., Hinchman, C., Forbes, C., Wang, J., Snider, N., Cordrey, A., Zhao, Y., Chandraratna, R.A. J. Biol. Chem. (2003) [Pubmed]
  31. The retinoic acid and brain-derived neurotrophic factor differentiated SH-SY5Y cell line as a model for Alzheimer's disease-like tau phosphorylation. Jämsä, A., Hasslund, K., Cowburn, R.F., Bäckström, A., Vasänge, M. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  32. Gene structure and alternative splicing of glycogen synthase kinase 3 beta (GSK-3beta) in neural and non-neural tissues. Schaffer, B., Wiedau-Pazos, M., Geschwind, D.H. Gene (2003) [Pubmed]
  33. PHF-tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase-3 beta. Mulot, S.F., Hughes, K., Woodgett, J.R., Anderton, B.H., Hanger, D.P. FEBS Lett. (1994) [Pubmed]
  34. RGS2 is an important target gene of Flt3-ITD mutations in AML and functions in myeloid differentiation and leukemic transformation. Schwäble, J., Choudhary, C., Thiede, C., Tickenbrock, L., Sargin, B., Steur, C., Rehage, M., Rudat, A., Brandts, C., Berdel, W.E., Müller-Tidow, C., Serve, H. Blood (2005) [Pubmed]
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