| pubmed-article:14507916 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0005507 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:14507916 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:14507916 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:14507916 | pubmed:dateCreated | 2003-11-24 | lld:pubmed |
| pubmed-article:14507916 | pubmed:abstractText | G protein-coupled receptor kinases (GRKs) specifically bind and phosphorylate the agonist-occupied form of G protein-coupled receptors. To further characterize the mechanism of GRK/receptor interaction, we developed a yeast-based bioassay using strains engineered to functionally express the somatostatin receptor subtype 2 and exhibit agonist-dependent growth. Here, we demonstrate that agonist-promoted growth was effectively inhibited by co-expression with either wild type GRK2 or GRK5, whereas catalytically inactive forms of these kinases were without effect. In an effort to identify residues involved in receptor interaction, we generated a pool of GRK5 mutants and then utilized the bioassay to identify mutants selectively deficient in inhibiting agonist-promoted growth. This resulted in the identification of a large number of mutants, several of which were expressed, purified, and characterized in more detail. Two of the mutants, GRK5-L3Q/K113R and GRK5-T10P, were defective in receptor phosphorylation and also exhibited a partial defect in phospholipid binding and phospholipid-stimulated autophosphorylation of the kinase. In contrast, these mutants had wild type activity in phosphorylating the non-receptor substrate tubulin. To further characterize the function of the NH2-terminal region of GRK5, we generated a deletion mutant lacking residues 2-14 and found that this mutant was also severely impaired in receptor phosphorylation and phospholipid-promoted autophosphorylation. In addition, an NH2-terminal 14-amino acid peptide from GRK5 selectively inhibited receptor phosphorylation by GRK5 but had minimal effect on GRK2 activity. Based on these findings, we propose a model whereby the extreme NH2 terminus of GRK5 mediates phospholipid binding and is required for optimal receptor phosphorylation. | lld:pubmed |
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| pubmed-article:14507916 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14507916 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14507916 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14507916 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:14507916 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14507916 | pubmed:author | pubmed-author:BenovicJeffre... | lld:pubmed |
| pubmed-article:14507916 | pubmed:author | pubmed-author:NobleBethB | lld:pubmed |
| pubmed-article:14507916 | pubmed:author | pubmed-author:KallalLorena... | lld:pubmed |
| pubmed-article:14507916 | pubmed:author | pubmed-author:PauschMark... | lld:pubmed |
| pubmed-article:14507916 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14507916 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:14507916 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:14507916 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14507916 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14507916 | pubmed:pagination | 47466-76 | lld:pubmed |
| pubmed-article:14507916 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:14507916 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14507916 | pubmed:articleTitle | Development of a yeast bioassay to characterize G protein-coupled receptor kinases. Identification of an NH2-terminal region essential for receptor phosphorylation. | lld:pubmed |
| pubmed-article:14507916 | pubmed:affiliation | Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. | lld:pubmed |
| pubmed-article:14507916 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14507916 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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