Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1824, Issue 1, Pages 113-122Publisher
ELSEVIER
DOI: 10.1016/j.bbapap.2011.06.005
Keywords
Apoptosis; Caspase; FLIP; Necroptosis; Receptor interacting protein kinase
Categories
Funding
- Netherlands Organization for Scientific Research (NWO)
- Barth Syndrome Foundation
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Caspase-8, the initiator of extrinsically-triggered apoptosis, also has important functions in cellular activation and differentiation downstream of a variety of cell surface receptors. It has become increasingly clear that the heterodimer of caspase-8 with the long isoform of cellular FLIP (FLIPL) fulfills these pro-survival functions of caspase-8. FLIPL, a catalytically defective caspase-8 paralog, can interact with caspase-8 to activate its catalytic function. The caspase-8/FLIPL heterodimer has a restricted substrate repertoire and does not induce apoptosis. In essence, caspase-8 heterodimerized with FLIPL prevents the receptor interacting kinases RIPK1 and -3 from executing the form of cell death known as necroptosis. This review discusses the latest insights in caspase-8 homo- versus heterodimerization and the implication this has for cellular death or survival. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome. (C) 2011 Elsevier B.V. All rights reserved.
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