| Ripped to death. | |
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MedLine Citation:
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PMID: 21978761 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Ricardo Weinlich; Christopher P Dillon; Douglas R Green |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-4 |
Journal Detail:
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Title: Trends in cell biology Volume: - ISSN: 1879-3088 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-7 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9200566 Medline TA: Trends Cell Biol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Ltd. |
Affiliation:
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Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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