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Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction.

Serum and glucocorticoid-inducible kinase-like kinase (SGKL) has been identified as a new integrator that decodes lipid signals produced by the activation of phosphoinositide 3-kinase (PI3K). SGKL is activated via its lipid-binding domain (phox homology domain) in response to PI3K signaling. However, downstream targets of SGKL as well as the role of SGKL as a mediator in PI3K signaling in human tissues remain to be established. In this study, we identified human glycogen synthase kinase 3 beta (GSK-3beta) as a specific interacting partner with SGKL in a yeast two-hybrid screening of human brain cDNA library. The association between these two proteins is confirmed independently in human embryonic kidney (HEK293) cells by co-immunoprecipitation. Furthermore, the kinase activity of wild-type SGKL was required for the in vitro phosphorylation of a GSK-3 crosstide fusion protein at serine-21/9 as demonstrated with a Phospho-GSK-3alpha/beta (Ser21/9) specific antibody. The present results provide strong evidences that SGKL could utilize GSK-3beta as a direct downstream target by phosphorylating GSK-3beta at serine-9.

Pubmed ID: 12054501


  • Dai F
  • Yu L
  • He H
  • Chen Y
  • Yu J
  • Yang Y
  • Xu Y
  • Ling W
  • Zhao S


Biochemical and biophysical research communications

Publication Data

May 17, 2002

Associated Grants


Mesh Terms

  • Brain
  • Calcium-Calmodulin-Dependent Protein Kinases
  • DNA, Complementary
  • Gene Library
  • Glycogen Synthase Kinase 3
  • Glycogen Synthase Kinases
  • Humans
  • Phosphatidylinositol 3-Kinases
  • Phosphorylation
  • Plasmids
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Serine
  • Signal Transduction
  • Two-Hybrid System Techniques