| Literature DB >> 15280015 |
Teija L T Aho1, Jouko Sandholm, Katriina J Peltola, Harri P Mankonen, Michael Lilly, Päivi J Koskinen.
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.Entities:
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Year: 2004 PMID： 15280015 DOI： 10.1016/j.febslet.2004.06.050
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124