Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/67127
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Type: Journal article
Title: Cytokine receptor signaling activates an IKK-dependent phosphorylation of PUMA to prevent cell death
Author: Sandow, J.
Jabbour, A.
Condina, M.
Daunt, C.
Stomski, F.
Green, B.
Riffkin, C.
Hoffmann, P.
Guthridge, M.
Silke, J.
Lopez, A.
Ekert, P.
Citation: Cell Death and Differentiation, 2012; 19(4):633-641
Publisher: Nature Publishing Group
Issue Date: 2012
ISSN: 1350-9047
1476-5403
Statement of
Responsibility: 
JJ Sandow, AM Jabbour, MR Condina, CP Daunt, FC Stomski, BD Green, CD Riffkin, P Hoffmann, MA Guthridge, J Silke, AF Lopez and PG Ekert
Abstract: P53-upregulated modifier of apoptosis (PUMA), a pro-apoptotic member of the Bcl-2 family, is transcriptionally activated by p53 and is a key effector of p53-dependent apoptosis. We show that PUMA protein is subject to rapid post-translational regulation by phosphorylation at a conserved residue, serine 10, following serum or interleukin-3 (IL-3) stimulation. Serine 10 is not within the Bcl-2 homology (BH3) domain, and PUMA phosphorylated at serine 10 retained the ability to co-immunoprecipitate with antiapoptotic Bcl-2 family members. However, phosphorylated PUMA was targeted for proteasomal degradation indicating that it is less stable than unphosphorylated PUMA. Importantly, we identified IKK1/IKK2/Nemo as the kinase complex that interacts with and phosphorylates PUMA, thereby also demonstrating that IL-3 activates NFκB signaling. The identification and characterization of this novel survival pathway has important implications for IL-3 signaling and hematopoietic cell development.
Keywords: PUMA; interleukin-3; post-translational; phosphorylation; degradation; IKK
Rights: Copyright 2011 Macmillan Publishers Limited
RMID: 0020117313
DOI: 10.1038/cdd.2011.131
Appears in Collections:IPAS publications

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