pubmed-article:17200117 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C0330386 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C0282114 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C0289793 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C1624581 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C1998811 | lld:lifeskim |
pubmed-article:17200117 | lifeskim:mentions | umls-concept:C1293132 | lld:lifeskim |
pubmed-article:17200117 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:17200117 | pubmed:dateCreated | 2007-2-26 | lld:pubmed |
pubmed-article:17200117 | pubmed:abstractText | Gravin (AKAP12) is a membrane-associated scaffold that provides docking for protein kinases, phosphatases, and adaptor molecules obligate for resensitization and recycling of beta(2)-adrenergic receptors. Gravin binds to the cell membrane in a Ca(2+)-sensitive manner and to receptors through well characterized protein-protein interactions. Although the interaction of serine/threonine, cyclic AMP-dependent protein kinase with protein kinase A-anchoring proteins is well described and involves a kinase regulatory subunit binding domain in the C terminus of these proteins, far less is known about tyrosine kinase docking to members of this family of scaffolds. The non-receptor tyrosine kinase Src regulates resensitization of beta(2)-adrenergic receptors and docks to gravin. Gravin displays nine proline-rich domains distributed throughout the molecule. One class I ligand for Src homology domain 3 docking, found in the N terminus ((10)RXPXXP(15)) of gravin, is shown to bind Src. Binding of Src to gravin activates the intrinsic tyrosine kinase of Src. Mutagenesis/deletion of the class I ligand (P15A,P16A) on the N terminus of gravin abolishes both the docking of Src to gravin as well as the receptor resensitization and recycling catalyzed by gravin. The Src-binding peptide-(1-51) of gravin behaves as a dominant-negative for AKAP gravin regulation of receptor resensitization/recycling. The tyrosine kinase Src plays an essential role in the AKAP gravin-mediated receptor resensitization and recycling, an essential aspect of receptor biology. | lld:pubmed |
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pubmed-article:17200117 | pubmed:language | eng | lld:pubmed |
pubmed-article:17200117 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17200117 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17200117 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17200117 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17200117 | pubmed:month | Mar | lld:pubmed |
pubmed-article:17200117 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:17200117 | pubmed:author | pubmed-author:WangHsien-YuH... | lld:pubmed |
pubmed-article:17200117 | pubmed:author | pubmed-author:TaoJiangchuan... | lld:pubmed |
pubmed-article:17200117 | pubmed:author | pubmed-author:MalbonCraig... | lld:pubmed |
pubmed-article:17200117 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17200117 | pubmed:day | 2 | lld:pubmed |
pubmed-article:17200117 | pubmed:volume | 282 | lld:pubmed |
pubmed-article:17200117 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17200117 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17200117 | pubmed:pagination | 6597-608 | lld:pubmed |
pubmed-article:17200117 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:17200117 | pubmed:meshHeading | pubmed-meshheading:17200117... | lld:pubmed |
pubmed-article:17200117 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17200117 | pubmed:articleTitle | Src docks to A-kinase anchoring protein gravin, regulating beta2-adrenergic receptor resensitization and recycling. | lld:pubmed |
pubmed-article:17200117 | pubmed:affiliation | Department of Pharmacology, State University of New York, Stony Brook, New York 11794-8651, USA. | lld:pubmed |
pubmed-article:17200117 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17200117 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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