| pubmed-article:16186509 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C0012691 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C0230770 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C0751283 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C0185115 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:16186509 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:16186509 | pubmed:issue | 40 | lld:pubmed |
| pubmed-article:16186509 | pubmed:dateCreated | 2005-10-7 | lld:pubmed |
| pubmed-article:16186509 | pubmed:abstractText | Polypeptides that fail to pass quality control in the endoplasmic reticulum (ER) are dislocated from the ER membrane to the cytosol where they are degraded by the proteasome. Derlin-1, a member of a family of proteins that bears homology to yeast Der1p, was identified as a factor that is required for the human cytomegalovirus US11-mediated dislocation of class I MHC heavy chains from the ER membrane to the cytosol. Derlin-1 acts in concert with the AAA ATPase p97 to remove dislocation substrate proteins from the ER membrane, but it is unknown whether other factors aid Derlin-1 in its function. Mammalian genomes encode two additional, related proteins (Derlin-2 and Derlin-3). The similarity of the mammalian Derlin-2 and Derlin-3 proteins to yeast Der1p suggested that these as-yet-uncharacterized Derlins also may play a role in ER protein degradation. We demonstrate here that Derlin-2 is an ER-resident protein that, similar to Derlin-1, participates in the degradation of proteins from the ER. Furthermore, we show that Derlin-2 forms a robust multiprotein complex with the p97 AAA ATPase as well as the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex. The data presented here define a set of interactions between proteins involved in dislocation of misfolded polypeptides from the ER. | lld:pubmed |
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| pubmed-article:16186509 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16186509 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16186509 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16186509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16186509 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16186509 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16186509 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16186509 | pubmed:author | pubmed-author:PloeghHidde... | lld:pubmed |
| pubmed-article:16186509 | pubmed:author | pubmed-author:LilleyBrendan... | lld:pubmed |
| pubmed-article:16186509 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16186509 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:16186509 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:16186509 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16186509 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16186509 | pubmed:pagination | 14296-301 | lld:pubmed |
| pubmed-article:16186509 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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