FEBS Letters · 2004 · 320 citations · 30 references
Life SciencesCell BiologyMolecular BiologyApoptosisCell SignalingSignal TransductionApoptosis ModulationApoptosis RegulationApoptotic Signal TransductionApoptotic SignalingBcl-2 Family ProteinsCytokine BiologyApoptosis Regulation By KinasesBcl-2 Protein ExpressionCytokine-induced ApoptosisPro-apoptotic Bcl-2 ProteinsPro-apoptotic EffectorsPro-apoptotic ProteinsProapoptotic Protein RegulationProapoptotic Protein Signaling
Constitutive expression of the Pim-1 kinase prolongs survival of cytokine-deprived FDCP1 cells, partly via maintenance of Bcl-2 expression. Here, we show that Pim-1 colocalizes and physically interacts with the pro-apoptotic Bad protein and phosphorylates it in vitro on serine 112, which is a gatekeeper site for its inactivation. Furthermore, wild-type Pim-1, but not a kinase-deficient mutant, enhances phosphorylation of this site in FDCP1 cells and protects cells from the pro-apoptotic effects of Bad. Our results suggest that phosphorylation of Bad by Pim-1 is one of several mechanisms via which the Pim-1 kinase can enhance Bcl-2 activity and promote cell survival.
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Interleukin-3-Induced Phosphorylation of BAD Through the Protein Kinase Akt
Luis del Peso, Maribel González-Garcı́a, Carmen Page et al. · Science · 1997 · 2.2K citations