| pubmed-article:16168377 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0010222 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0020374 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0023689 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C1332083 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:16168377 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:16168377 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16168377 | pubmed:dateCreated | 2005-9-19 | lld:pubmed |
| pubmed-article:16168377 | pubmed:abstractText | Sterol-regulated ubiquitination is an obligatory step in ER-associated degradation (ERAD) of HMG CoA reductase, a rate-limiting enzyme in cholesterol synthesis. Accelerated degradation of reductase, one of several strategies animal cells use to limit production of cholesterol, requires sterol-induced binding of the enzyme to ER membrane proteins called Insigs. Once formed, the reductase-Insig complex is recognized by a putative membrane-associated ubiquitin ligase (E3) that mediates the reductase ubiquitination reaction. Here, we show that gp78, a membrane bound E3, binds to Insig-1 and is required for sterol-regulated ubiquitination of reductase. In addition, gp78 couples regulated ubiquitination to degradation of reductase by binding to VCP, an ATPase that plays a key role in recognition and degradation of ERAD substrates. The current results identify gp78 as the E3 that initiates sterol-accelerated degradation of reductase, and Insig-1 as a bridge between gp78/VCP and the reductase substrate. | lld:pubmed |
| pubmed-article:16168377 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16168377 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16168377 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16168377 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16168377 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16168377 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16168377 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16168377 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16168377 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16168377 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:16168377 | pubmed:author | pubmed-author:SongBao-Liang... | lld:pubmed |
| pubmed-article:16168377 | pubmed:author | pubmed-author:SeverNavdarN | lld:pubmed |
| pubmed-article:16168377 | pubmed:author | pubmed-author:DeBose-BoydRu... | lld:pubmed |
| pubmed-article:16168377 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16168377 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:16168377 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:16168377 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16168377 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16168377 | pubmed:pagination | 829-40 | lld:pubmed |
| pubmed-article:16168377 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16168377 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16168377 | pubmed:articleTitle | Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. | lld:pubmed |
| pubmed-article:16168377 | pubmed:affiliation | Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA. | lld:pubmed |
| pubmed-article:16168377 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16168377 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16168377 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16168377 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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