pubmed-article:17635908 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
pubmed-article:17635908 | lifeskim:mentions | umls-concept:C1947906 | lld:lifeskim |
pubmed-article:17635908 | pubmed:issue | 40 | lld:pubmed |
pubmed-article:17635908 | pubmed:dateCreated | 2007-10-1 | lld:pubmed |
pubmed-article:17635908 | pubmed:abstractText | After activation, most G protein-coupled receptors (GPCRs) are regulated by a cascade of events involving desensitization and endocytosis. Internalized receptors can then be recycled to the plasma membrane, retained in an endosomal compartment, or targeted for degradation. The GPCR-associated sorting protein, GASP, has been shown to preferentially sort a number of native GPCRs to the lysosome for degradation after endocytosis. Here we show that a mutant beta(2) adrenergic receptor and a mutant mu opioid receptor that have previously been described as lacking "recycling signals" due to mutations in their C termini in fact bind to GASP and are targeted for degradation. We also show that a mutant dopamine D1 receptor, which has likewise been described as lacking a recycling signal, does not bind to GASP and is therefore not targeted for degradation. Together, these results indicate that alteration of receptors in their C termini can expose determinants with affinity for GASP binding and consequently target receptors for degradation. | lld:pubmed |
pubmed-article:17635908 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:language | eng | lld:pubmed |
pubmed-article:17635908 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17635908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17635908 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17635908 | pubmed:month | Oct | lld:pubmed |
pubmed-article:17635908 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:17635908 | pubmed:author | pubmed-author:WhistlerJenni... | lld:pubmed |
pubmed-article:17635908 | pubmed:author | pubmed-author:ThompsonDawnD | lld:pubmed |
pubmed-article:17635908 | pubmed:author | pubmed-author:PuschMargaret... | lld:pubmed |
pubmed-article:17635908 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17635908 | pubmed:day | 5 | lld:pubmed |
pubmed-article:17635908 | pubmed:volume | 282 | lld:pubmed |
pubmed-article:17635908 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17635908 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17635908 | pubmed:pagination | 29178-85 | lld:pubmed |
pubmed-article:17635908 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
pubmed-article:17635908 | pubmed:meshHeading | pubmed-meshheading:17635908... | lld:pubmed |
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pubmed-article:17635908 | pubmed:meshHeading | pubmed-meshheading:17635908... | lld:pubmed |
pubmed-article:17635908 | pubmed:meshHeading | pubmed-meshheading:17635908... | lld:pubmed |
pubmed-article:17635908 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17635908 | pubmed:articleTitle | Changes in G protein-coupled receptor sorting protein affinity regulate postendocytic targeting of G protein-coupled receptors. | lld:pubmed |
pubmed-article:17635908 | pubmed:affiliation | Ernest Gallo Clinic and Research Center, University of California, San Francisco, Emeryville, California 94608, USA. | lld:pubmed |
pubmed-article:17635908 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17635908 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:17635908 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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