| pubmed-article:10719047 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10719047 | lifeskim:mentions | umls-concept:C0682972 | lld:lifeskim |
| pubmed-article:10719047 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:10719047 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:10719047 | lifeskim:mentions | umls-concept:C1514648 | lld:lifeskim |
| pubmed-article:10719047 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:10719047 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10719047 | pubmed:dateCreated | 2000-3-31 | lld:pubmed |
| pubmed-article:10719047 | pubmed:abstractText | We have previously shown that not only G protein-coupled receptor kinase (GRK) 2, but also a catalytically inactive Lys220Trp GRK2 decreases endothelin (ET)-1-induced inositol 1,4,5-trisphosphate (IP3) formation, and demonstrated the presence of phosphorylation-independent desensitization mechanism. To clarify the role of GRK2 other than that as a kinase, we characterized an RGS (regulator of G protein signaling)-like domain in the amino-terminus of GRK2. Both GRK2(1-181) and GRK2(54-174) suppressed Ca2+ responses induced by angiotensin II (Ang II) and ET-1, and bound directly with Galphaq but not Galphas nor Galphai3 in the presence of GDP and AlF4-. These results demonstrate that GRK2 regulates Gq-mediated signaling negatively by direct interaction between its RGS domain and the transitional state of Galphaq, as well as through phosphorylation of activated receptors by its kinase domain. | lld:pubmed |
| pubmed-article:10719047 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10719047 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10719047 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10719047 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10719047 | pubmed:issn | 1107-3756 | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:MorozZZ | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:IshidaJJ | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:KimuraSS | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:KAWAM ZMZ | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:SekiyaSS | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:ShibasakiTT | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:FukamizuAA | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:NishiyamaMM | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:UsuiHH | lld:pubmed |
| pubmed-article:10719047 | pubmed:author | pubmed-author:ZhouJJ | lld:pubmed |
| pubmed-article:10719047 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10719047 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:10719047 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10719047 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10719047 | pubmed:pagination | 335-40 | lld:pubmed |
| pubmed-article:10719047 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:10719047 | pubmed:meshHeading | pubmed-meshheading:10719047... | lld:pubmed |
| pubmed-article:10719047 | pubmed:meshHeading | pubmed-meshheading:10719047... | lld:pubmed |
| pubmed-article:10719047 | pubmed:meshHeading | pubmed-meshheading:10719047... | lld:pubmed |
| pubmed-article:10719047 | pubmed:meshHeading | pubmed-meshheading:10719047... | lld:pubmed |
| pubmed-article:10719047 | pubmed:meshHeading | pubmed-meshheading:10719047... | lld:pubmed |
| pubmed-article:10719047 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10719047 | pubmed:articleTitle | RGS domain in the amino-terminus of G protein-coupled receptor kinase 2 inhibits Gq-mediated signaling. | lld:pubmed |
| pubmed-article:10719047 | pubmed:affiliation | Department of Biochemistry and Molecular Pharmacology, Chiba University Graduate, School of Medicine, Chuo-ku, Chiba 260-8670, Japan. | lld:pubmed |
| pubmed-article:10719047 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10719047 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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