| pubmed-article:16987818 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C1332083 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C1421437 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C1414357 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:16987818 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:16987818 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:16987818 | pubmed:dateCreated | 2006-11-13 | lld:pubmed |
| pubmed-article:16987818 | pubmed:abstractText | Improperly folded proteins in the endoplasmic reticulum (ER) are eliminated via ER-associated degradation, a process that dislocates misfolded proteins from the ER membrane into the cytosol, where they undergo proteasomal degradation. Dislocation requires a subclass of ubiquitin ligases that includes gp78 in addition to the AAA ATPase p97/VCP and its cofactor, the Ufd1-Npl4 dimer. We have previously reported that gp78 interacts directly with p97/VCP. Here, we identify a novel p97/VCP-interacting motif (VIM) within gp78 that mediates this interaction. We demonstrate that the VIM of gp78 recruits p97/VCP to the ER, but has no effect on Ufd1 localization. We also show that gp78 VIM interacts with the ND1 domain of p97/VCP that was shown previously to be the binding site for Ufd1. To evaluate the role of Ufd1 in gp78-p97/VCP-mediated degradation of CD3delta, a known substrate of gp78, RNA interference was used to silence the expression of Ufd1 and p97/VCP. Inhibition of p97/VCP, but not Ufd1, stabilized CD3delta in cells that overexpress gp78. However, both p97/VCP and Ufd1 appear to be required for CD3delta degradation in cells expressing physiological levels of gp78. These results raise the possibility that Ufd1 and gp78 may bind p97/VCP in a mutually exclusive manner and suggest that gp78 might act in a Ufd1-independent degradation pathway for misfolded ER proteins, which operates in parallel with the previously established p97/VCP-Ufd1-Npl4-mediated mechanism. | lld:pubmed |
| pubmed-article:16987818 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16987818 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16987818 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16987818 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16987818 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16987818 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16987818 | pubmed:author | pubmed-author:YangHuiH | lld:pubmed |
| pubmed-article:16987818 | pubmed:author | pubmed-author:FangShengyunS | lld:pubmed |
| pubmed-article:16987818 | pubmed:author | pubmed-author:ShenYuxianY | lld:pubmed |
| pubmed-article:16987818 | pubmed:author | pubmed-author:BallarPetekP | lld:pubmed |
| pubmed-article:16987818 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16987818 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:16987818 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:16987818 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16987818 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16987818 | pubmed:pagination | 35359-68 | lld:pubmed |
| pubmed-article:16987818 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16987818 | pubmed:meshHeading | pubmed-meshheading:16987818... | lld:pubmed |
| pubmed-article:16987818 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16987818 | pubmed:articleTitle | The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation. | lld:pubmed |
| pubmed-article:16987818 | pubmed:affiliation | Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, Maryland 21201, USA. | lld:pubmed |
| pubmed-article:16987818 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16987818 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16987818 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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