期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 73, 期 11-12, 页码 2165-2176出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-016-2191-4
关键词
Ubiquitination; Necroptosis; TNFR1; RIPK1; c IAP1/2; LUBAC; A20; CYLD
Tumor necrosis factor (TNF) is a master pro-inflammatory cytokine, and inappropriate TNF signaling is implicated in the pathology of many inflammatory diseases. Ligation of TNF to its receptor TNFR1 induces the transient formation of a primary membrane-bound signaling complex, known as complex I, that drives expression of pro-survival genes. Defective complex I activation results in induction of cell death, in the form of apoptosis or necroptosis. This switch occurs via internalization of complex I components and assembly and activation of secondary cytoplasmic death complexes, respectively known as complex II and necrosome. In this review, we discuss the crucial regulatory functions of ubiquitination-a post-translational protein modification consisting of the covalent attachment of ubiquitin, and multiples thereof, to target proteins-to the various steps of TNFR1 signaling leading to necroptosis.
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