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http://purl.uniprot.org/citations/27321670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27321670http://www.w3.org/2000/01/rdf-schema#comment"Misfolded proteins of the ER are retrotranslocated to the cytosol, where they are polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To investigate how the ER-associated Degradation (ERAD) machinery can accomplish retrotranslocation of a misfolded luminal protein domain across a lipid bilayer, we have reconstituted retrotranslocation with purified S. cerevisiae proteins, using proteoliposomes containing the multi-spanning ubiquitin ligase Hrd1. Retrotranslocation of the luminal domain of a membrane-spanning substrate is triggered by autoubiquitination of Hrd1. Substrate ubiquitination is a subsequent event, and the Cdc48 ATPase that completes substrate extraction from the membrane is not required for retrotranslocation. Ubiquitination of lysines in Hrd1's RING-finger domain is required for substrate retrotranslocation in vitro and for ERAD in vivo. Our results suggest that Hrd1 forms a ubiquitin-gated protein-conducting channel."xsd:string
http://purl.uniprot.org/citations/27321670http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2016.05.048"xsd:string
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/author"Rapoport T.A."xsd:string
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/author"Baldridge R.D."xsd:string
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/pages"394-407"xsd:string
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/title"Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD."xsd:string
http://purl.uniprot.org/citations/27321670http://purl.uniprot.org/core/volume"166"xsd:string
http://purl.uniprot.org/citations/27321670http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27321670
http://purl.uniprot.org/citations/27321670http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27321670
http://purl.uniprot.org/uniprot/Q08109#attribution-BEBAD39446F09ED76FABC3392DA9E69Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/27321670
http://purl.uniprot.org/uniprot/#_P40318-mappedCitation-27321670http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27321670
http://purl.uniprot.org/uniprot/#_P38307-mappedCitation-27321670http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27321670
http://purl.uniprot.org/uniprot/#_Q08109-mappedCitation-27321670http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27321670
http://purl.uniprot.org/uniprot/P38307http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27321670
http://purl.uniprot.org/uniprot/P40318http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27321670
http://purl.uniprot.org/uniprot/Q08109http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/27321670