Document Detail


Ripped to death.
MedLine Citation:
PMID:  21978761     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
An old puzzle in the field of cell death was solved recently: the mysterious embryonic lethality of animals deficient in caspase-8 or Fas-associated death domain (FADD), proteins involved in a pathway of apoptosis. This lethality is caused by a failure to develop the yolk sac vasculature rather than a lack of apoptosis. Remarkably, development is rescued by ablation of either of two receptor interacting serine-threonine kinases (RIPKs). Despite being well known cell killers, caspase-8 and FADD act together to block RIPK-mediated necrosis. To manifest this newly elucidated pro-survival function, FADD and caspase-8 depend on FLIP(Long), a catalytically inactive caspase-8 homolog. In this review, the mechanism by which RIPK necrotic death is inhibited by this trio is discussed, as well as how RIPKs might themselves mediate cell death.
Authors:
Ricardo Weinlich; Christopher P Dillon; Douglas R Green
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-10-4
Journal Detail:
Title:  Trends in cell biology     Volume:  -     ISSN:  1879-3088     ISO Abbreviation:  -     Publication Date:  2011 Oct 
Date Detail:
Created Date:  2011-10-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9200566     Medline TA:  Trends Cell Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011. Published by Elsevier Ltd.
Affiliation:
Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
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