Poly-ubiquitination in TNFR1-mediated necroptosis.

Poly-ubiquitination in TNFR1-mediated necroptosis.
Cell Mol Life Sci. 2016 Apr 11;
Authors: Dondelinger Y, Darding M, Bertrand MJ, Walczak H
Abstract
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.
PMID: 27066894 [PubMed - as supplied by publisher]

Source: Cellular and Molecular Life Sciences : CMLS - April 10, 2016 Category: Cytology Authors: Dondelinger Y, Darding M, Bertrand MJ, Walczak H Tags: Cell Mol Life Sci Source Type: research