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 .
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