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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6596
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pubmed:dateCreated |
1996-10-3
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pubmed:databankReference | |
pubmed:abstractText |
Polypeptides that define a protein family termed RGS (for regulators of G-protein signalling) are encoded by the SST2 gene of the yeast Saccharomyces cerevisiae, the EGL-10 gene of the nematode Caenorhabdatis elegans, and several related mammalian genes. Genetic studies in invertebrates and mammalian cell-transfection experiments indicate that RGS proteins negatively regulate signalling pathways involving seven transmembrane receptors and heterotrimeric G proteins. However, the biochemical mechanism by which RGS proteins control these pathways is unknown. Here we report the characterization of human RGS10, a member of this protein family. Co-immunoprecipitation studies demonstrate that RGS10 associates specifically with the activated forms of two related G-protein subunits, G alphai3, and G alphaz, but fails to interact with the structurally and functionally distinct G alphas subunit. In vitro assays with purified proteins indicate that RGS10 increases potently and selectively the GTP hydrolytic activity of several members of the G alphai family, including G alphai3, G alphaz, and G alpha0. These results demonstrate that RGS proteins can attenuate signalling pathways involving heterotrimeric G proteins by serving as GTPase-activating proteins for specific types of G alpha subunits.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
383
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
175-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8774883-Amino Acid Sequence,
pubmed-meshheading:8774883-Animals,
pubmed-meshheading:8774883-Cloning, Molecular,
pubmed-meshheading:8774883-Enzyme Activation,
pubmed-meshheading:8774883-GTP Phosphohydrolases,
pubmed-meshheading:8774883-GTP-Binding Proteins,
pubmed-meshheading:8774883-Guanosine Triphosphate,
pubmed-meshheading:8774883-HeLa Cells,
pubmed-meshheading:8774883-Humans,
pubmed-meshheading:8774883-Hydrolysis,
pubmed-meshheading:8774883-Molecular Sequence Data,
pubmed-meshheading:8774883-Precipitin Tests,
pubmed-meshheading:8774883-Proteins,
pubmed-meshheading:8774883-RGS Proteins,
pubmed-meshheading:8774883-Rats,
pubmed-meshheading:8774883-Sequence Homology, Amino Acid,
pubmed-meshheading:8774883-Signal Transduction
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pubmed:year |
1996
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pubmed:articleTitle |
RGS10 is a selective activator of G alpha i GTPase activity.
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pubmed:affiliation |
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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