title: Ubiquitin-binding domains: mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin-modified proteomes.
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.
authors.affiliation: School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, UK.
authors.forename: Daniel
authors.initials: D
authors.lastname: Scott
authors.forename: Neil J
authors.initials: NJ
authors.lastname: Oldham
authors.forename: Jo
authors.initials: J
authors.lastname: Strachan
authors.forename: Mark S
authors.initials: MS
authors.lastname: Searle
authors.forename: Robert
authors.initials: R
authors.lastname: Layfield
mesh_terms: D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D006801:Humans; D051379:Mice; D017434:Protein Structure, Tertiary; D040901:Proteomics; D058615:Synthetic Biology; D025801:Ubiquitin
chemical_list: D025801:Ubiquitin
keywords: Synthetic biology; Technology; Ubiquitin; Ubiquitin-binding domain