A1 Refereed original research article in a scientific journal

Pim-1 kinase promotes inactivation of the pro-apoptotic bad protein by phosphorylating it on the Ser(112) gatekeeper site




AuthorsAho TLT, Sandholm J, Peltola KJ, Mankonen HP, Lilly M, Koskinen PJ

PublisherELSEVIER SCIENCE BV

Publication year2004

JournalFEBS Letters

Journal name in sourceFEBS LETTERS

Journal acronymFEBS LETT

Volume571

Issue1-3

First page 43

Last page49

Number of pages7

ISSN0014-5793

DOIhttps://doi.org/10.1016/j.febslet.2004.06.050


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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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