Abstract
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-3β) 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-3α/β (Ser21/9) specific antibody. The present results provide strong evidences that SGKL could utilize GSK-3β as a direct downstream target by phosphorylating GSK-3β at serine-9.
Original language | English (US) |
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Pages (from-to) | 1191-1196 |
Number of pages | 6 |
Journal | Biochemical and biophysical research communications |
Volume | 293 |
Issue number | 4 |
DOIs | |
State | Published - 2002 |
Keywords
- GSK-3β
- Inhibitory regulation
- PI3K signal pathway
- Phosphorylation
- SGKL
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology