| pubmed-article:10339594 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10339594 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:10339594 | lifeskim:mentions | umls-concept:C1419377 | lld:lifeskim |
| pubmed-article:10339594 | lifeskim:mentions | umls-concept:C1749432 | lld:lifeskim |
| pubmed-article:10339594 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:10339594 | pubmed:dateCreated | 1999-6-24 | lld:pubmed |
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| pubmed-article:10339594 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10339594 | pubmed:abstractText | Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain Galpha subunits and thereby modulate a number of G protein-dependent signaling cascades. Currently, little is known about the regulation of RGS proteins themselves. We identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome pathway. The degradation of RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic kidney disease. Furthermore, membranous expression of C-terminal polycystin relocalized RGS7. Our results indicate that rapid degradation and interaction with integral membrane proteins are potential means of regulating RGS proteins. | lld:pubmed |
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| pubmed-article:10339594 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10339594 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10339594 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10339594 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10339594 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10339594 | pubmed:month | May | lld:pubmed |
| pubmed-article:10339594 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:WalzGG | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:KimEE | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:BenzingTT | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:SukhatmeV PVP | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:ArnouldTT | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:KocherOO | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:TsiokasLL | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:ComellaNN | lld:pubmed |
| pubmed-article:10339594 | pubmed:author | pubmed-author:SellinLL | lld:pubmed |
| pubmed-article:10339594 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10339594 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10339594 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10339594 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10339594 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10339594 | pubmed:pagination | 6371-6 | lld:pubmed |
| pubmed-article:10339594 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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