Polyubiquitin binding and disassembly by deubiquitinating enzymes

• Authors: Francisca E. Reyes-Turcu, Emory University; Keith D. Wilkinson, Emory University
• Journal Title: Chemical Reviews
• Volume: Volume 109, Number 4
• Publisher: American Chemical Society | 2009-04, Pages 1495-1508
• Type of Work: Article | Post-print: After Peer Review
• Publisher DOI: http://doi.org/10.1021/cr800470j
• Subjects: Chemistry, Biochemistry
• Keywords: Deubiquitinating enzymes; polyubiquitin; ubiquitin isoforms; substrate recognition; ubiquitin receptors

Abstract

Ubiquitin (Ub) is a highly conserved protein of 76 amino acids that is covalently linked to target proteins altering their localization, function, or stability. Proteins can be modified with a large number of different isoforms of ubiquitin and these different ubiquitins are thought to signal different outcomes. The question of how these different forms of ubiquitin are recognized is central to understanding the specificity of various types of ubiquitination.