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Gene Review

gskt  -  gasket

Drosophila melanogaster

Synonyms: BEST:GH16447, BcDNA:AT21229, CG11338, CG31003, CT4237, ...
 
 
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Disease relevance of gskt

 

High impact information on gskt

  • The study of the substrate specificity and regulation of GSK3 activity has been important in the quest for therapeutic intervention [2].
  • LiCl, which specifically inhibits glycogen synthase kinase-3 (GSK-3), reduced Eve phosphorylation in nuclear extract and blocked inhibition of repression [3].
  • Here we show that two forms of GSK-3 function to decrease the DNA-binding activity as well as the transcriptional activation elicited by c-Jun in vivo [4].
  • The sgg proteins share homology with the mammalian GSK-3 and appear to be important for the normal segregation of bristle precursor cells in the imaginal epithelium in Drosophila [4].
  • We determined that WRM-1 and the major canonical Wnt pathway components: BAR-1, SGG-1/GSK-3 and PRY-1/Axin were not involved in the control of B cell polarity [5].
 

Chemical compound and disease context of gskt

 

Biological context of gskt

  • Higher plants contain a multigene family encoding proteins that share a highly conserved catalytic protein kinase domain about 70% identical to SHAGGY protein kinase (SGG) and glycogen synthase kinase-3 (GSK-3), respectively, from Drosophila and mammals [6].
  • The cDNA cloning also revealed a striking degree of amino acid identity between the two GSK-3 proteins, particularly the beta-form, and the zeste-white3/shaggy (zw3sgg) homeotic gene of Drosophila melanogaster [7].
 

Associations of gskt with chemical compounds

  • GSK-3, a ubiquitous kinase regulated by tyrosine phosphorylation, controls cell-fate decisions in both Drosophila and Dictyostelium; genetic analysis of its interactions with other signaling pathways is now possible [8].
 

Analytical, diagnostic and therapeutic context of gskt

References

  1. Arabidopsis homologs of the shaggy and GSK-3 protein kinases: molecular cloning and functional expression in Escherichia coli. Bianchi, M.W., Guivarc'h, D., Thomas, M., Woodgett, J.R., Kreis, M. Mol. Gen. Genet. (1994) [Pubmed]
  2. The renaissance of GSK3. Cohen, P., Frame, S. Nat. Rev. Mol. Cell Biol. (2001) [Pubmed]
  3. Allosteric regulation of even-skipped repression activity by phosphorylation. Li, C., Manley, J.L. Mol. Cell (1999) [Pubmed]
  4. Negative regulation of Jun/AP-1: conserved function of glycogen synthase kinase 3 and the Drosophila kinase shaggy. de Groot, R.P., Auwerx, J., Bourouis, M., Sassone-Corsi, P. Oncogene (1993) [Pubmed]
  5. A novel noncanonical Wnt pathway is involved in the regulation of the asymmetric B cell division in C. elegans. Wu, M., Herman, M.A. Dev. Biol. (2006) [Pubmed]
  6. The Arabidopsis SHAGGY-related protein kinase (ASK) gene family: structure, organization and evolution. Dornelas, M.C., Lejeune, B., Dron, M., Kreis, M. Gene (1998) [Pubmed]
  7. Baculovirus-mediated expression and characterisation of rat glycogen synthase kinase-3 beta, the mammalian homologue of the Drosophila melanogaster zeste-white 3sgg homeotic gene product. Hughes, K., Pulverer, B.J., Theocharous, P., Woodgett, J.R. Eur. J. Biochem. (1992) [Pubmed]
  8. Intercellular signaling. A kinase for cell-fate determination? Briscoe, C., Firtel, R.A. Curr. Biol. (1995) [Pubmed]
  9. Identification of multifunctional ATP-citrate lyase kinase as the alpha-isoform of glycogen synthase kinase-3. Hughes, K., Ramakrishna, S., Benjamin, W.B., Woodgett, J.R. Biochem. J. (1992) [Pubmed]
 
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