Mechanisms for regulating deubiquitinating enzymes. (12th February 2014)

• Record Type: Journal Article
• Authors: Wolberger, Cynthia
• Is Part Of: Protein science. Volume 23:Number 4(2014:Apr.)
• Page Start: 344
• Page End: 353
• Publication Date: 2014-02-12
• Subjects: ubiquitin -- deubiquitinating enzymes -- UBL -- DUB; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.2415
• Languages: English
• ISSNs: 0961-8368

Abstract

Abstract: Ubiquitination is a reversible post‐translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N‐termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated.