Ontology highlight
ABSTRACT:
SUBMITTER: Abdul Rehman SA
PROVIDER: S-EPMC4942677 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Abdul Rehman Syed Arif SA Kristariyanto Yosua Adi YA Choi Soo-Youn SY Nkosi Pedro Junior PJ Weidlich Simone S Labib Karim K Hofmann Kay K Kulathu Yogesh Y
Molecular cell 20160609 1
Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitylation. Here we report the discovery of a new family of DUBs, which we have named MINDY (motif interacting with Ub-containing novel DUB family). Found in all eukaryotes, MINDY-family DUBs are highly selective at cleaving K48-linked polyUb, a signal that targets proteins for degradation. We identify the catalytic activity to be encoded within a previously unannotated d ...[more]