3-Phosphoinositide-dependent protein kinase 1 (PDK1) is a serine/threonine protein kinase known to phosphorylate and activate various signal transduction pathways: Akt/PKB (Thr308 and Ser473), p70 S6 kinase, RSK, PKA, PKC, and SGK. Upon stimulation of receptor tyrosine kinases, PI3K becomes activated and generates the phospholipid second messengers, PtdIns(3,4,5)P3 and PtdIns(3,4)P2, which in turn mediate the phosphorylation and activation of PDK1 targets through diverse mechanisms (1, 2). Unlike other phosphorylation sites on PDK1, only phosphorylation on the activation loop at Ser241 is necessary for PDK1 activity; a single mutation to Ala abolishes its activity (3). PDK1 can also autophosphorylate Ser241, leading to its own activation (3).
Signaling by GPCR
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