QIK is a serine/threonine protein kinase that contains an N-terminal kinase domain, a central domain with ubiquitin-associate motif, and a C-terminal PKA phosphorylation site. QIK can phosphorylate IRS1 and overexpression of QIK in adipocyte elevates the phosphorylation of IRS1. The QIK-mediated phosphorylation of IRS1 may modulate the efficiency of insulin signal transduction and could be responsible for insulin resistance associated with diabetes. Insulin disrupts TORC2 activity by induction of QIK which then stimulates the phosphorylation and cytoplasmic translocation of TORC2. Phosphorylated TORC2 is subsequently degraded by the 26S proteasome.
During feeding, increases in circulating pancreatic insulin inhibit hepatic glucose output through the activation of the Ser/Thr kinase AKT and subsequent phosphorylation of the forkhead transcription factor FOXO1 (refs 1-3). Under fasting conditions, FOXO1 increases gluconeogenic gene expression in concert
The Journal of biological chemistry, 278(20), 18440-18447 (2003-03-08)
Salt-inducible kinase (SIK), first cloned from the adrenal glands of rats fed a high salt diet, is a serine/threonine protein kinase belonging to an AMP-activated protein kinase family. Induced in Y1 cells at an early stage of ACTH stimulation, it
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