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http://purl.uniprot.org/citations/22689655http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22689655http://www.w3.org/2000/01/rdf-schema#comment"Little is known about quality control of proteins that aberrantly or persistently engage the endoplasmic reticulum (ER)-localized translocon en route to membrane localization or the secretory pathway. Hrd1 and Doa10, the primary ubiquitin ligases that function in ER-associated degradation (ERAD) in yeast, target distinct subsets of misfolded or otherwise abnormal proteins based primarily on degradation signal (degron) location. We report the surprising observation that fusing Deg1, a cytoplasmic degron normally recognized by Doa10, to the Sec62 membrane protein rendered the protein a Hrd1 substrate. Hrd1-dependent degradation occurred when Deg1-Sec62 aberrantly engaged the Sec61 translocon channel and underwent topological rearrangement. Mutations that prevent translocon engagement caused a reversion to Doa10-dependent degradation. Similarly, a variant of apolipoprotein B, a protein known to be cotranslocationally targeted for proteasomal degradation, was also a Hrd1 substrate. Hrd1 therefore likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the translocon."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201203061"xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/author"Rubenstein E.M."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/author"Swanson R."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/author"Kreft S.G."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/author"Greenblatt W."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/pages"761-773"xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/title"Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase."xsd:string
http://purl.uniprot.org/citations/22689655http://purl.uniprot.org/core/volume"197"xsd:string
http://purl.uniprot.org/citations/22689655http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22689655
http://purl.uniprot.org/citations/22689655http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22689655
http://purl.uniprot.org/uniprot/#_P40318-mappedCitation-22689655http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22689655
http://purl.uniprot.org/uniprot/#_Q08109-mappedCitation-22689655http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22689655
http://purl.uniprot.org/uniprot/#_P21825-mappedCitation-22689655http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22689655
http://purl.uniprot.org/uniprot/P40318http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22689655
http://purl.uniprot.org/uniprot/P21825http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22689655
http://purl.uniprot.org/uniprot/Q08109http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22689655