Ubiquitin‐binding domains: Mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin‐modified proteomes. Issue 5 (28th December 2014)

• Record Type: Journal Article
• Authors: Scott, Daniel; Oldham, Neil J.; Strachan, Jo; Searle, Mark S.; Layfield, Robert
• Editors: Dunn, Michael J.
• Is Part Of: Proteomics. Volume 15:Issue 5/6(2015:Mar.)
• Page Start: 844
• Page End: 861
• Publication Date: 2014-12-28
• Subjects: Synthetic biology -- Technology -- Ubiquitin -- Ubiquitin‐binding domain; Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201400341
• Languages: English
• ISSNs: 1615-9853

Abstract

Abstract : Ubiquitin‐binding domains (UBDs) are modular units found within ubiquitin‐binding proteins that mediate the non‐covalent recognition of (poly)ubiquitin modifications. A variety of mechanisms are employed in vivo to achieve polyubiquitin linkage and chain length selectivity by UBDs, the structural basis of which have in some instances been determined. Here, we review current knowledge related to ubiquitin recognition mechanisms at the molecular level and explore how such information has been exploited in the design and application of UBDs in isolation or artificially arranged in tandem as tools to investigate ubiquitin‐modified proteomes. Specifically, we focus on the use of UBDs to directly purify or detect (poly)ubiquitin‐modified proteins and more broadly for the targeted manipulation of ubiquitin‐mediated processes, highlighting insights into ubiquitin signalling that have been provided.