{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Piatkov KI"],"funding":["NIDDK NIH HHS","NIGMS NIH HHS"],"pagination":["926-33"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3889152"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["48(6)"],"pubmed_abstract":["Deamidation of N-terminal Gln by the Ntaq1 Nt(Q)-amidase is a part of the Arg/N-end rule pathway, a ubiquitin-dependent proteolytic system. Here we identify Gln-Usp1(Ct), the C-terminal fragment of the autocleaved Usp1 deubiquitylase, as the first physiological Arg/N-end rule substrate that is targeted for degradation through deamidation of N-terminal Gln. Usp1 regulates genomic stability, in part through the deubiquitylation of monoubiquitylated PCNA, a DNA polymerase processivity factor. The autocleaved Usp1 remains a deubiquitylase because its fragments remain associated with Uaf1, an enhancer of Usp1 activity, until the Gln-Usp1(Ct) fragment is selectively destroyed by the Arg/N-end rule pathway. We also show that metabolic stabilization of Gln-Usp1(Ct) results in a decreased monoubiqu"],"journal":["Molecular cell"],"pubmed_title":["The auto-generated fragment of the Usp1 deubiquitylase is a physiological substrate of the N-end rule pathway."],"pmcid":["PMC3889152"],"funding_grant_id":["R56 DK039520","R01 GM031530","DK039520","GM084244","R01 GM084244","GM031530","R01 DK039520","R37 DK039520"],"pubmed_authors":["Varshavsky A","Colnaghi L","Huang TT","Piatkov KI","Bekes M"],"additional_accession":[]},"is_claimable":false,"name":"The auto-generated fragment of the Usp1 deubiquitylase is a physiological substrate of the N-end rule pathway.","description":"Deamidation of N-terminal Gln by the Ntaq1 Nt(Q)-amidase is a part of the Arg/N-end rule pathway, a ubiquitin-dependent proteolytic system. Here we identify Gln-Usp1(Ct), the C-terminal fragment of the autocleaved Usp1 deubiquitylase, as the first physiological Arg/N-end rule substrate that is targeted for degradation through deamidation of N-terminal Gln. Usp1 regulates genomic stability, in part through the deubiquitylation of monoubiquitylated PCNA, a DNA polymerase processivity factor. The autocleaved Usp1 remains a deubiquitylase because its fragments remain associated with Uaf1, an enhancer of Usp1 activity, until the Gln-Usp1(Ct) fragment is selectively destroyed by the Arg/N-end rule pathway. We also show that metabolic stabilization of Gln-Usp1(Ct) results in a decreased monoubiqu","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Dec","modification":"2025-04-04T21:13:32.295Z","creation":"2019-03-27T01:19:53Z"},"accession":"S-EPMC3889152","cross_references":{"pubmed":["23159736"],"doi":["10.1016/j.molcel.2012.10.012"]}}