Insights into ubiquitin chain architecture using Ub-clipping.

ABSTRACT: Protein ubiquitination is a multi-functional post-translational modification that affects all cellular processes. Its versatility arises from architecturally complex polyubiquitin chains, in which individual ubiquitin moieties may be ubiquitinated on one or multiple residues, and/or modified by phosphorylation and acetylation^1-3. Advances in mass spectrometry have enabled the mapping of individual ubiquitin modifications that generate the ubiquitin code; however, the architecture of polyubiquitin signals has remained largely inaccessible. Here we introduce Ub-clipping as a methodology by which to understand polyubiquitin signals and architectures. Ub-clipping uses an engineered viral protease, Lb^pro∗, to incompletely remove ubiquitin from substrates and leave the sign

SUBMITTER: Swatek KN 

PROVIDER: S-EPMC6823057 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature