期刊
BIOCHEMICAL JOURNAL
卷 400, 期 -, 页码 235-244出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20060905
关键词
cell survival; C-terminus of Hsc70 interacting protein (CHIP) E3 ligase; serum and glucocorticoid-regulated kinase-1 (SGK-1); stress response; phosphoinositide 3-kinase (PI3K); ubiquitination
资金
- NCI NIH HHS [CA014599-31, R01 CA089208, P30 CA014599, CA90459, K08 CA090459, CA89208] Funding Source: Medline
SGK-1 (serum- and glucocorticoid-regulatedkinase-1) is a stress-induced serine/threonine kinase that is phosphorylated and activated downstream of PI3K (phosphoinositide 3-kinase). SGK-1 plays a critical role in insulin signalling, cation transport and cell survival. SGK-1 mRNA expression is transiently induced following cellular stress, and SGK-1 protein levels are tightly regulated by rapid proteasomal degradation. In the present study we report that SGK-1 forms a complex with the stress-associated E3 ligase CHIP [C-terminus of Hsc (heat-shock cognate protein) 70-interacting protein]; CHIP is requited for both the ubiquitin modification and rapid proteasomal degradation of SGK-1. We also show that CHIP co-localizes with SGK-1 at or near the endoplasmic reticulum. CHIP-mediated regulation of SGK-1 steadystate levels alters SGK-1 kinase activity. These data suggest a model that integrates CHIP function with regulation of the PI3K/SGK-1 pathway in the stress response.
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