| pubmed-article:12738775 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C0184512 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C1418835 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:12738775 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:12738775 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:12738775 | pubmed:dateCreated | 2003-8-18 | lld:pubmed |
| pubmed-article:12738775 | pubmed:abstractText | The third intracellular (3i) loops of the alpha 2A- and alpha 2B-adrenergic receptor (AR) subtypes are critical for retention of these receptors at the basolateral surface of polarized Madin-Darby canine kidney (MDCKII) cells at steady state. The third intracellular loops of the alpha 2A, alpha 2B, and alpha 2C-AR subtypes interact with spinophilin, a multidomain protein that, like the three alpha 2-AR subtypes, is enriched at the basolateral surface of MDCKII cells. The present studies provide evidence that alpha 2-AR interaction with spinophilin contributes to cell surface stabilization of the receptor. We exploited the unique targeting profile of the alpha 2B-AR subtype in MDCKII cells: random delivery to apical and basolateral surfaces with rapid (t(1/2) < or = 60 min) apical versus slower (t(1/2) = 10-12 h) basolateral turnover. Apical delivery of a spinophilin subdomain containing the alpha 2-AR-interacting region (Sp151-483) by fusion with apically targeted p75NTR extended the half-life of alpha 2B-AR at the apical surface to approximately 3.6 h and eliminated the rapid phase (0-60 min) of alpha 2B-AR turnover on that surface. Furthermore, we examined alpha 2B-AR turnover at the surface of mouse embryo fibroblasts derived from wild type (Sp+/+) or spinophilin knock-out (Sp-/-) mice. Two independent experimental approaches demonstrated that agonist-evoked internalization of HA-alpha 2B-AR was accelerated in mouse embryo fibroblasts derived from Sp-/- mice. These findings are consistent with the interpretation that endogenous spinophilin contributes to the stabilization of alpha 2B-AR and presumably all three alpha2-AR subtypes at the surface of target cells and may act as a scaffold that could link alpha 2-ARs to proteins interacting with spinophilin via other domains. | lld:pubmed |
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| pubmed-article:12738775 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12738775 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12738775 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12738775 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12738775 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12738775 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12738775 | pubmed:author | pubmed-author:LimbirdLee... | lld:pubmed |
| pubmed-article:12738775 | pubmed:author | pubmed-author:WangQinQ | lld:pubmed |
| pubmed-article:12738775 | pubmed:author | pubmed-author:GreengardPaul... | lld:pubmed |
| pubmed-article:12738775 | pubmed:author | pubmed-author:BradyAshley... | lld:pubmed |
| pubmed-article:12738775 | pubmed:author | pubmed-author:AllenPatrick... | lld:pubmed |
| pubmed-article:12738775 | pubmed:author | pubmed-author:ColbranRoger... | lld:pubmed |
| pubmed-article:12738775 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12738775 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:12738775 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12738775 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12738775 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12738775 | pubmed:pagination | 32405-12 | lld:pubmed |
| pubmed-article:12738775 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12738775 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12738775 | pubmed:articleTitle | Spinophilin stabilizes cell surface expression of alpha 2B-adrenergic receptors. | lld:pubmed |
| pubmed-article:12738775 | pubmed:affiliation | Department of Pharmacology, Center for Molecular Neuroscience, Vanderbilt University Medical Center, Nashville, Tennessee 37232-6600, USA. | lld:pubmed |
| pubmed-article:12738775 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12738775 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12738775 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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