Biochem J 2006,
PMID: 16895519
Belova, Larissa; Sharma, Sanjay; Brickley, Deanna R; Nicolarsen, Jeremy R; Patterson, Cam; Conzen, Suzanne D
SGK-1 (serum- and glucocorticoid-regulated kinase-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 required 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 steady-state 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.
Diseases/Pathways annotated by Medline MESH: Breast Neoplasms
Document information provided by NCBI PubMed
Text Mining Data
insulin — SGK-1: "
SGK-1 plays a critical role in
insulin signalling, cation transport and cell survival
"
Manually curated Databases
-
IRef Biogrid Interaction:
UBC
—
SGK1
(physical association, affinity chromatography technology)
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IRef Biogrid Interaction:
HSPA4
—
SGK1
(physical association, affinity chromatography technology)
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IRef Biogrid Interaction:
STUB1
—
SGK1
(physical association, affinity chromatography technology)
In total, 3 gene pairs are associated to this article in curated databases