The 3-phosphoinositide-dependent protein kinase 1 (PDK1 or A0260) is a serine/threonine protein kinase of the AGC group, PKB family.
The 3-phosphoinositide-dependent protein kinase 1 (PDK1 or A0260) is a serine/threonine protein kinase of the AGC group, PKB family. It is considered a master regulatory kinase because of its capacity to phosphorylate and activate a variety of AGC protein kinases, including Akt, P70S6K, protein kinase A (PKA), ribosomal S6 kinase (RSK) and several protein kinase C (PKC) isozymes. This allows PDK1 to modulate the activity of multiple signaling pathways, including cell proliferation, cell size, development, differentiation, apoptosis and insulin receptor signaling. The Insulin receptor-dependent activation of the Akt pathway, through PI3K, is one of the best-characterized mechanisms of PDK1 kinase modulation. It is proposed that the constitutive binding and phosphorylation of PKMζ by PDK1, facilitates the persistent activity of PKMζ and the maintenance of long-term potentiation (LTP). PDK1 is ubiquitously expressed and null mice die at embryonic day 9.5, presenting multiple abnormalities.