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Immunol Rev. 2012 Mar;246(1):107-24. doi: 10.1111/j.1600-065X.2012.01100.x.

Regulation of NF-κB by deubiquitinases.

Author information

1
Department of Microbiology and Immunology, Sylvester Comprehensive Cancer Center, The University of Miami, Miller School of Medicine, Miami, FL, USA.

Abstract

The nuclear factor-κB (NF-κB) pathway is a critical regulator of innate and adaptive immunity. Noncanonical K63-linked polyubiquitination plays a key regulatory role in NF-κB signaling pathways by functioning as a scaffold to recruit kinase complexes containing ubiquitin-binding domains. Ubiquitination is balanced by deubiquitinases that cleave polyubiquitin chains and oppose the function of E3 ubiquitin ligases. Deubiquitinases therefore play an important role in the termination of NF-κB signaling and the resolution of inflammation. In this review, we focus on NF-κB regulation by deubiquitinases with an emphasis on A20 and CYLD. Deubiquitinases and the ubiquitin/proteasome components that regulate NF-κB may serve as novel therapeutic targets for inflammatory diseases and cancer.

PMID:
22435550
PMCID:
PMC3540820
DOI:
10.1111/j.1600-065X.2012.01100.x
[Indexed for MEDLINE]
Free PMC Article

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