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http://purl.uniprot.org/citations/16449189http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16449189http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16449189http://www.w3.org/2000/01/rdf-schema#comment"Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. Components of both productive folding and ER-associated degradation (ERAD) mechanisms are known to be up-regulated by the unfolded protein response (UPR). We describe two novel components of mammalian ERAD, Derlin-2 and -3, which show weak homology to Der1p, a transmembrane protein involved in yeast ERAD. Both Derlin-2 and -3 are up-regulated by the UPR, and at least Derlin-2 is a target of the IRE1 branch of the response, which is known to up-regulate ER degradation enhancing alpha-mannosidase-like protein (EDEM) and EDEM2, receptor-like molecules for misfolded glycoprotein. Overexpression of Derlin-2 or -3 accelerated degradation of misfolded glycoprotein, whereas their knockdown blocked degradation. Derlin-2 and -3 are associated with EDEM and p97, a cytosolic ATPase responsible for extraction of ERAD substrates. These findings indicate that Derlin-2 and -3 provide the missing link between EDEM and p97 in the process of degrading misfolded glycoproteins."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200507057"xsd:string
http://purl.uniprot.org/citations/16449189http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200507057"xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Oda Y."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Oda Y."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Mori K."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Mori K."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Okada T."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Okada T."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Yoshida H."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Yoshida H."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Nagata K."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Nagata K."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Kaufman R.J."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/author"Kaufman R.J."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/pages"383-393"xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/pages"383-393"xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/title"Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."xsd:string
http://purl.uniprot.org/citations/16449189http://purl.uniprot.org/core/title"Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."xsd:string