http://purl.uniprot.org/citations/19394298 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19394298 | http://www.w3.org/2000/01/rdf-schema#comment | "Quality control pathways such as ER-associated degradation (ERAD) employ a small number of factors to specifically recognize a wide variety of protein substrates. Delineating the mechanisms of substrate selection is a principle goal in studying quality control. The Hrd1p ubiquitin ligase mediates ERAD of numerous misfolded proteins including soluble, lumenal ERAD-L and membrane-anchored ERAD-M substrates. We tested if the Hrd1p multispanning membrane domain was involved in ERAD-M specificity. In this work, we have identified site-directed membrane domain mutants of Hrd1p impaired only for ERAD-M and normal for ERAD-L. Furthermore, other Hrd1p variants were specifically deficient for degradation of individual ERAD-M substrates. Thus, the Hrd1p transmembrane region bears determinants of high specificity in the ERAD-M pathway. From in vitro and interaction studies, we suggest a model in which the Hrd1p membrane domain employs intramembrane residues to evaluate substrate misfolding, leading to selective ubiquitination of appropriate ERAD-M clients."xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2009.03.010"xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/author | "Schulz D."xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/author | "Hampton R.Y."xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/author | "Sato B.K."xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/author | "Do P.H."xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/name | "Mol Cell"xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/pages | "212-222"xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/title | "Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase."xsd:string |
http://purl.uniprot.org/citations/19394298 | http://purl.uniprot.org/core/volume | "34"xsd:string |
http://purl.uniprot.org/citations/19394298 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19394298 |
http://purl.uniprot.org/citations/19394298 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19394298 |
http://purl.uniprot.org/uniprot/#_Q08109-mappedCitation-19394298 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19394298 |
http://purl.uniprot.org/uniprot/#_P12684-mappedCitation-19394298 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19394298 |
http://purl.uniprot.org/uniprot/Q08109 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19394298 |
http://purl.uniprot.org/uniprot/P12684 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19394298 |