Phosphorylation-dependent substrate selectivity of protein kinase B (AKT1)
Nileeka Balasuriya, Norman E. Davey, Jared L. Johnson, Huadong Liu, Kyle K. Biggar, Lewis C. Cantley, Shawn S.‐C. Li, Patrick O’Donoghue
Abstract
, the addition of Ser-473 phosphorylation increased AKT1 activities on some, but not all of its substrates. This is the first report that Ser-473 phosphorylation can positively or negatively regulate kinase activity in a substrate-dependent fashion. Bioinformatics analysis indicated that the OPAL-activity data effectively discriminate known AKT1 substrates from closely related kinase substrates. Our results also enabled predictions of novel AKT1 substrates that suggest new and expanded roles for AKT1 signaling in regulating cellular processes.
Topics & Concepts
AKT1PhosphorylationKinaseBiologySignal transductionCell biologyChemistryProtein kinase BPI3K/AKT/mTOR signaling in cancerChemical Synthesis and AnalysisProtein Degradation and Inhibitors