PIKKing on PKB: regulation of PKB activity by phosphorylation
L Bozulic, BA Hemmings - Current opinion in cell biology, 2009 - Elsevier
L Bozulic, BA Hemmings
Current opinion in cell biology, 2009•ElsevierSer/Thr protein kinase PKB/Akt is a key regulator of a wide range of cellular processes
including growth, proliferation and survival. PKB is clearly a crucial signaling molecule and
extensive research efforts aim to understand its regulation and action. Recent studies of the
regulation of PKB activity by hydrophobic motif phosphorylation have yielded several
exciting findings about members of the PI3-kinase-like family of kinases (PIKKs) acting as
PKB regulators. Mammalian target of rapamycin complex 2 (mTORC2) and DNA-dependent …
including growth, proliferation and survival. PKB is clearly a crucial signaling molecule and
extensive research efforts aim to understand its regulation and action. Recent studies of the
regulation of PKB activity by hydrophobic motif phosphorylation have yielded several
exciting findings about members of the PI3-kinase-like family of kinases (PIKKs) acting as
PKB regulators. Mammalian target of rapamycin complex 2 (mTORC2) and DNA-dependent …
Ser/Thr protein kinase PKB/Akt is a key regulator of a wide range of cellular processes including growth, proliferation and survival. PKB is clearly a crucial signaling molecule and extensive research efforts aim to understand its regulation and action. Recent studies of the regulation of PKB activity by hydrophobic motif phosphorylation have yielded several exciting findings about members of the PI3-kinase-like family of kinases (PIKKs) acting as PKB regulators. Mammalian target of rapamycin complex 2 (mTORC2) and DNA-dependent protein kinase (DNA-PK) can both phosphorylate Ser473 and activate PKB. This present review concerns PKB regulation by mTORC2 and DNA-PK in a stimulus-dependent and context-dependent manner and the possible implications of this for PKB activity, substrate specificity and therapeutic intervention.
Elsevier