| Ripoptosome: a novel IAP-regulated cell death-signalling platform. | |
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MedLine Citation:
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PMID: 22114055 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Cell death is indispensable for normal growth and development of multicellular organisms. Caspases, the effector proteases of apoptosis are normally activated by dimerization in multimeric protein complexes and inhibitors of apoptosis (IAPs) function as endogenous inhibitors of caspases. Recent studies have revealed that cell death stimuli can also trigger programmed necrosis, necroptosis. Receptor-interacting serine-threonine kinase family RIP plays a crucial role in regulating the switch between apoptosis and necroptosis. Two studies now describe a novel RIP1 containing ∼2 MDa 'Ripoptosome' complex assembled in the cytosol to mediate both apoptosis and necroptosis in response to genotoxic stress and TLR3 stimulation. Intriguingly, cIAPs and XIAP function as endogenous inhibitors of Ripoptosome by direct ubiquitination of its components. These studies shed further light into the molecular mechanisms behind RIP kinase-regulated cell death and open new avenues for therapeutic intervention of various pathologies including cancer. |
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Authors:
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Gergely Imre; Sarit Larisch; Krishnaraj Rajalingam |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-23 |
Journal Detail:
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Title: Journal of molecular cell biology Volume: - ISSN: 1759-4685 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-24 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101503669 Medline TA: J Mol Cell Biol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Institute of Biochemistry II, Goethe University School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt am Main, Germany. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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