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CYLD: a tumor suppressor deubiquitinase regulating NF-κB activation and diverse biological processes

CYLD: a tumor suppressor deubiquitinase regulating NF-κB activation and diverse biological processes Protein ubiquitination is a reversible reaction, in which the ubiquitin chains are deconjugated by a family of deubiquitinases (DUBs). The presence of a large number of DUBs suggests that they likely possess certain levels of substrate selectivity and functional specificity. Indeed, recent studies show that a tumor suppressor DUB, cylindromatosis (CYLD), has a predominant role in the regulation of NF-κB, a transcription factor that promotes cell survival and oncogenesis. NF-κB activation involves attachment of K63-linked ubiquitin chains to its upstream signaling factors, which is thought to facilitate protein–protein interactions in the assembly of signaling complexes. By deconjugating these K63-linked ubiquitin chains, CYLD negatively regulates NF-κB activation, which may contribute to its tumor suppressor function. CYLD also regulates diverse physiological processes, ranging from immune response and inflammation to cell cycle progression, spermatogenesis, and osteoclastogenesis. Interestingly, CYLD itself is subject to different mechanisms of regulation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cell Death & Differentiation Springer Journals

CYLD: a tumor suppressor deubiquitinase regulating NF-κB activation and diverse biological processes

Sun, S-C
Cell Death & Differentiation , Volume 17 (1) – Apr 17, 2009
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References (113)

Publisher
Springer Journals
Copyright
Copyright © 2010 by Macmillan Publishers Limited
Subject
Life Sciences; Life Sciences, general; Biochemistry, general; Cell Biology; Stem Cells; Apoptosis; Cell Cycle Analysis
ISSN
1350-9047
eISSN
1476-5403
DOI
10.1038/cdd.2009.43
Publisher site
See Article on Publisher Site

Abstract

Protein ubiquitination is a reversible reaction, in which the ubiquitin chains are deconjugated by a family of deubiquitinases (DUBs). The presence of a large number of DUBs suggests that they likely possess certain levels of substrate selectivity and functional specificity. Indeed, recent studies show that a tumor suppressor DUB, cylindromatosis (CYLD), has a predominant role in the regulation of NF-κB, a transcription factor that promotes cell survival and oncogenesis. NF-κB activation involves attachment of K63-linked ubiquitin chains to its upstream signaling factors, which is thought to facilitate protein–protein interactions in the assembly of signaling complexes. By deconjugating these K63-linked ubiquitin chains, CYLD negatively regulates NF-κB activation, which may contribute to its tumor suppressor function. CYLD also regulates diverse physiological processes, ranging from immune response and inflammation to cell cycle progression, spermatogenesis, and osteoclastogenesis. Interestingly, CYLD itself is subject to different mechanisms of regulation.

Journal

Cell Death & Differentiation – Springer Journals

Published: Apr 17, 2009

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