{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Que LT"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["921-932"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7761795"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["59(8)"],"pubmed_abstract":["OTUB1 is a highly expressed cysteine protease that specifically cleaves K48-linked polyubiquitin chains. This unique deubiquitinating enzyme (DUB) can bind to a subset of E2 ubiquitin conjugating enzymes, forming complexes in which the two enzymes can regulate one another's activity. OTUB1 can noncatalytically suppress the ubiquitin conjugating activity of its E2 partners by sequestering the charged E2∼Ub thioester and preventing ubiquitin transfer. The same E2 enzymes, when uncharged, can stimulate the DUB activity of OTUB1 <i>in vitro</i>, although the importance of OTUB1 stimulation <i>in vivo</i> remains unclear. To assess the potential balance between these activities that might occur in cells, we characterized the kinetics and thermodynamics governing the formation and activity of OT"],"journal":["Biochemistry"],"pubmed_title":["Comparison of Cross-Regulation by Different OTUB1:E2 Complexes."],"pmcid":["PMC7761795"],"funding_grant_id":["GM109102","GM130393","R01 GM109102","R35 GM130393"],"pubmed_authors":["Que LT","Morrow ME","Wolberger C"],"additional_accession":[]},"is_claimable":false,"name":"Comparison of Cross-Regulation by Different OTUB1:E2 Complexes.","description":"OTUB1 is a highly expressed cysteine protease that specifically cleaves K48-linked polyubiquitin chains. This unique deubiquitinating enzyme (DUB) can bind to a subset of E2 ubiquitin conjugating enzymes, forming complexes in which the two enzymes can regulate one another's activity. OTUB1 can noncatalytically suppress the ubiquitin conjugating activity of its E2 partners by sequestering the charged E2∼Ub thioester and preventing ubiquitin transfer. The same E2 enzymes, when uncharged, can stimulate the DUB activity of OTUB1 <i>in vitro</i>, although the importance of OTUB1 stimulation <i>in vivo</i> remains unclear. To assess the potential balance between these activities that might occur in cells, we characterized the kinetics and thermodynamics governing the formation and activity of OT","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Mar","modification":"2026-05-02T13:22:10.574Z","creation":"2021-03-05T09:09:05Z"},"accession":"S-EPMC7761795","cross_references":{"pubmed":["32049508"],"doi":["10.1021/acs.biochem.9b00993"]}}