[HTML][HTML] Pim-1 kinase promotes inactivation of the pro-apoptotic Bad protein by phosphorylating it on the Ser112 gatekeeper site
TLT Aho, J Sandholm, KJ Peltola, HP Mankonen… - FEBS letters, 2004 - Elsevier
TLT Aho, J Sandholm, KJ Peltola, HP Mankonen, M Lilly, PJ Koskinen
FEBS letters, 2004•ElsevierConstitutive 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 …
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 …
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.
Elsevier