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lüll Regulation of death receptor signaling by the ubiquitin system Wertz IE; Dixit VMCell Death Differ 2010[Jan]; 17 (1): 14-24The study of death receptor (DR) signaling has led to the discovery of new signaling paradigms, including the first example of direct receptor-mediated activation of a protease (caspase-8) that functions as a second messenger to initiate a 'death cascade' of downstream protease activation. More recently, this receptor system has underscored the importance of ubiquitin modification in NF-kappaB activation. Both degradative lysine 48-linked polyubiquitin and scaffolding lysine 63-linked polyubiquitin have an essential role in signal propagation. Remarkably, a negative feedback process, termed ubiquitin editing, regulates signaling that emanates from certain DRs. Ubiquitin editing is mediated by a complex interplay between the ubiquitination and deubiquitination machinery, resulting in the replacement of signal enhancing lysine 63-linked polyubiquitin with signal extinguishing lysine 48-linked polyubiquitin. The ubiquitination machinery and its regulation in the context of DR signaling are discussed herein.|CARD Signaling Adaptor Proteins/metabolism[MESH]|Caspase 8/metabolism[MESH]|Fas-Associated Death Domain Protein/metabolism[MESH]|Receptors, Death Domain/*metabolism[MESH]|Signal Transduction[MESH]|TNF Receptor-Associated Death Domain Protein/metabolism[MESH]|Ubiquitin/*metabolism[MESH]|Ubiquitination[MESH] |