A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Pim-1 kinase promotes inactivation of the pro-apoptotic bad protein by phosphorylating it on the Ser(112) gatekeeper site
Tekijät: Aho TLT, Sandholm J, Peltola KJ, Mankonen HP, Lilly M, Koskinen PJ
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 2004
Journal: FEBS Letters
Tietokannassa oleva lehden nimi: FEBS LETTERS
Lehden akronyymi: FEBS LETT
Vuosikerta: 571
Numero: 1-3
Aloitussivu: 43
Lopetussivu: 49
Sivujen määrä: 7
ISSN: 0014-5793
DOI: https://doi.org/10.1016/j.febslet.2004.06.050
Tiivistelmä
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.
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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