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https://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 |
DOI: | 10.1038/cdd.2011.131 |
Published version: | http://dx.doi.org/10.1038/cdd.2011.131 |
Appears in Collections: | Aurora harvest 5 IPAS publications |
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