Ontology highlight
ABSTRACT:
SUBMITTER: Morrow ME
PROVIDER: S-EPMC6172466 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
Morrow Marie E ME Morgan Michael T MT Clerici Marcello M Growkova Katerina K Yan Ming M Komander David D Sixma Titia K TK Simicek Michal M Wolberger Cynthia C
EMBO reports 20180827 10
A common strategy for exploring the biological roles of deubiquitinating enzymes (DUBs) in different pathways is to study the effects of replacing the wild-type DUB with a catalytically inactive mutant in cells. We report here that a commonly studied DUB mutation, in which the catalytic cysteine is replaced with alanine, can dramatically increase the affinity of some DUBs for ubiquitin. Overexpression of these tight-binding mutants thus has the potential to sequester cellular pools of monoubiqui ...[more]