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Regulation of ubiquitin‐dependent processes by deubiquitinating enzymes
Author(s) -
Wilkinson Keith D.
Publication year - 1997
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.11.14.9409543
Subject(s) - deubiquitinating enzyme , ubiquitin , proteases , enzyme , ubiquitins , microbiology and biotechnology , chemistry , ubiquitin ligase , biochemistry , biology , gene
An astounding number of important regulatory and structural proteins are subject to modification by the attachment of ubiquitin or ubiquitin‐like proteins. This modification acts as a targeting signal, delivering the modified protein to different locations in the cell and modifying its activity, macromolecular interactions, or half‐life. Deubiquitination, or the removal of this modification, is being recognized as an important regulatory strategy. This reaction is catalyzed by processing proteases known as deubiquitinating enzymes (DUBs). More than 60 DUBs are already known, although little is known about their biological roles. This review concentrates on recent findings and new insights into this fascinating class of enzymes.—Wilkinson, K. D. Regulation of ubiquitin‐dependent processes by deubiquitinating enzymes. FASEB J. 11, 1245–1256 (1997)