| pubmed-article:11588219 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11588219 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:11588219 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:11588219 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:11588219 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:11588219 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11588219 | lifeskim:mentions | umls-concept:C0167464 | lld:lifeskim |
| pubmed-article:11588219 | pubmed:issue | 5545 | lld:pubmed |
| pubmed-article:11588219 | pubmed:dateCreated | 2001-11-9 | lld:pubmed |
| pubmed-article:11588219 | pubmed:abstractText | Although trafficking and degradation of several membrane proteins are regulated by ubiquitination catalyzed by E3 ubiquitin ligases, there has been little evidence connecting ubiquitination with regulation of mammalian G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptor (GPCR) function. Agonist stimulation of endogenous or transfected beta2-adrenergic receptors (beta2ARs) led to rapid ubiquitination of both the receptors and the receptor regulatory protein, beta-arrestin. Moreover, proteasome inhibitors reduced receptor internalization and degradation, thus implicating a role for the ubiquitination machinery in the trafficking of the beta2AR. Receptor ubiquitination required beta-arrestin, which bound to the E3 ubiquitin ligase Mdm2. Abrogation of beta-arrestin ubiquitination, either by expression in Mdm2-null cells or by dominant-negative forms of Mdm2 lacking E3 ligase activity, inhibited receptor internalization with marginal effects on receptor degradation. However, a beta2AR mutant lacking lysine residues, which was not ubiquitinated, was internalized normally but was degraded ineffectively. These findings delineate an adapter role of beta-arrestin in mediating the ubiquitination of the beta2AR and indicate that ubiquitination of the receptor and of beta-arrestin have distinct and obligatory roles in the trafficking and degradation of this prototypic GPCR. | lld:pubmed |
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| pubmed-article:11588219 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11588219 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11588219 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11588219 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11588219 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:11588219 | pubmed:author | pubmed-author:LefkowitzR... | lld:pubmed |
| pubmed-article:11588219 | pubmed:author | pubmed-author:KohoutT ATA | lld:pubmed |
| pubmed-article:11588219 | pubmed:author | pubmed-author:ShenoyS KSK | lld:pubmed |
| pubmed-article:11588219 | pubmed:author | pubmed-author:McDonaldP HPH | lld:pubmed |
| pubmed-article:11588219 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11588219 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:11588219 | pubmed:volume | 294 | lld:pubmed |
| pubmed-article:11588219 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11588219 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11588219 | pubmed:pagination | 1307-13 | lld:pubmed |
| pubmed-article:11588219 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11588219 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11588219 | pubmed:articleTitle | Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. | lld:pubmed |
| pubmed-article:11588219 | pubmed:affiliation | Howard Hughes Medical Institute and Department of Medicine, Duke University Medical Center, Box 3821, Durham, NC 27710, USA. | lld:pubmed |
| pubmed-article:11588219 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11588219 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11588219 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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