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IKK{varepsilon} DEPENDENT PHOSPHORYLATION AND DEGRADATION OF X-LINKED INHIBITOR OF APOPTOSIS SENSITIZES CELLS TO VIRUS-INDUCED APOPTOSIS.
MedLine Citation:
PMID:  22072751     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
X-linked inhibitor of apoptosis (XIAP) is a potent antagonist of caspase-3, -7 and -9 dependent apoptotic activities that functions as an E3 ubiquitin ligase, and targets caspases for degradation. In this study, we demonstrate that Sendai virus (SeV) infection results in IKKε or TBK1-mediated phosphorylation of XIAP in vivo at Ser430, resulting in Lys(48)-linked autoubiquitination at Lys322/328 residues, followed by subsequent proteasomal degradation of XIAP. Interesting, IKKε expression and XIAP turnover increases SeV-triggered mitochondrial dependent apoptosis via release of caspase-3, whereas TBK1 expression does not increase apoptosis. Interestingly, phosphorylation also regulates XIAP interaction with the transcription factor IRF3, suggesting a role in IRF3-Bax mediated apoptosis. Our findings reveal a novel function of IKKε as a regulator of virus-induced triggering of apoptosis via phosphorylation-dependent turnover of XIAP.
Authors:
Peyman Nakhaei; Qiang Sun; Mayra Solis; Thibault Mesplede; Eric Bonneil; Suzanne Paz; Rongtuan Lin; John Hiscott
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-9
Journal Detail:
Title:  Journal of virology     Volume:  -     ISSN:  1098-5514     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, Jewish General Hospital.
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