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http://purl.uniprot.org/citations/32327568http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32327568http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32327568http://www.w3.org/2000/01/rdf-schema#comment"Misfolded luminal endoplasmic reticulum (ER) proteins undergo ER-associated degradation (ERAD-L): They are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. ERAD-L is mediated by the Hrd1 complex (composed of Hrd1, Hrd3, Der1, Usa1, and Yos9), but the mechanism of retrotranslocation remains mysterious. Here, we report a structure of the active Hrd1 complex, as determined by cryo-electron microscopy analysis of two subcomplexes. Hrd3 and Yos9 jointly create a luminal binding site that recognizes glycosylated substrates. Hrd1 and the rhomboid-like Der1 protein form two "half-channels" with cytosolic and luminal cavities, respectively, and lateral gates facing one another in a thinned membrane region. These structures, along with crosslinking and molecular dynamics simulation results, suggest how a polypeptide loop of an ERAD-L substrate moves through the ER membrane."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.org/dc/terms/identifier"doi:10.1126/science.aaz2449"xsd:string
http://purl.uniprot.org/citations/32327568http://purl.org/dc/terms/identifier"doi:10.1126/science.aaz2449"xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Liao M."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Liao M."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Mi W."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Mi W."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Nudler E."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Nudler E."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Wu X."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Rapoport T.A."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Rapoport T.A."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Hummer G."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Hummer G."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Ovchinnikov S."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Ovchinnikov S."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Siggel M."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Siggel M."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Svetlov V."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/author"Svetlov V."xsd:string
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32327568http://purl.uniprot.org/core/date"2020"xsd:gYear