FEBS Lett. 2004 Jul 30;571(1-3):43-9.

Pim-1 kinase promotes inactivation of the pro-apoptotic Bad protein by phosphorylating it on the Ser112 gatekeeper site.

Aho TL, Sandholm J, Peltola KJ, Mankonen HP, Lilly M, Koskinen PJ.

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Turku Centre for Biotechnology, University of Turku/Abo Akademi University, Tykistökatu 6 B, 20520 Turku, Finland.

Abstract

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.

PMID:: 15280015; [PubMed - indexed for MEDLINE]

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Pim-1 kinase promotes inactivation of the pro-apoptotic Bad protein by phosphorylating it on the Ser112 gatekeeper site.

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