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



Authors: Aho TLT, Sandholm J, Peltola KJ, Mankonen HP, Lilly M, Koskinen PJ

Publisher: ELSEVIER SCIENCE BV

Publication year: 2004

Journal: FEBS Letters

Journal name in source: FEBS LETTERS

Journal acronym: FEBS LETT

Volume: 571

Issue: 1-3

First page : 43

Last page: 49

Number of pages: 7

ISSN: 0014-5793

DOI: https://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.

Downloadable publication

This is an electronic reprint of the original article.
This reprint may differ from the original in pagination and typographic detail. Please cite the original version.


Last updated on 2024-26-11 at 19:46