Control of Akt activity and substrate phosphorylation in cells
Ivan Yudushkin
Abstract
Protein kinase B/Akt is a serine/threonine kinase that links receptors coupled to the PI3K lipid kinase to cellular anabolic pathways. Its activity in cells is controlled by reversible phosphorylation and an intramolecular lipid-controlled allosteric switch. In this review, I outline the current progress in understanding Akt regulatory mechanisms, define three models of Akt activation in cells, and highlight how intramolecular allosterism cooperates with cell-autonomous mechanisms to control Akt localization and activity and direct it toward specific sets of substrates in cells.
Topics & Concepts
Protein kinase BPhosphorylationCell biologyAllosteric regulationPI3K/AKT/mTOR pathwayChemistryKinaseProto-Oncogene Proteins c-aktSignal transductionBiochemistryBiologyReceptorPI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase SignalingPolyamine Metabolism and Applications