| http://purl.uniprot.org/citations/18264092 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18264092 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18264092 | http://www.w3.org/2000/01/rdf-schema#comment | "Terminally misfolded or unassembled proteins in the early secretory pathway are degraded by a ubiquitin- and proteasome-dependent process known as ER-associated degradation (ERAD). How substrates of this pathway are recognized within the ER and delivered to the cytoplasmic ubiquitin-conjugating machinery is unknown. We report here that OS-9 and XTP3-B/Erlectin are ER-resident glycoproteins that bind to ERAD substrates and, through the SEL1L adaptor, to the ER-membrane-embedded ubiquitin ligase Hrd1. Both proteins contain conserved mannose 6-phosphate receptor homology (MRH) domains, which are required for interaction with SEL1L, but not with substrate. OS-9 associates with the ER chaperone GRP94 which, together with Hrd1 and SEL1L, is required for the degradation of an ERAD substrate, mutant alpha(1)-antitrypsin. These data suggest that XTP3-B and OS-9 are components of distinct, partially redundant, quality control surveillance pathways that coordinate protein folding with membrane dislocation and ubiquitin conjugation in mammalian cells."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb1689"xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.org/dc/terms/identifier | "doi:10.1038/ncb1689"xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Kopito R.R."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Kopito R.R."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Tyler R.E."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Tyler R.E."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Christianson J.C."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Christianson J.C."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Shaler T.A."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/author | "Shaler T.A."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/name | "Nat. Cell Biol."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/pages | "272-282"xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/pages | "272-282"xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/title | "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/title | "OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD."xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/volume | "10"xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://purl.uniprot.org/core/volume | "10"xsd:string |
| http://purl.uniprot.org/citations/18264092 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18264092 |
| http://purl.uniprot.org/citations/18264092 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18264092 |