Source:http://linkedlifedata.com/resource/pubmed/id/12618216
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2003-3-5
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pubmed:abstractText |
Regulators of G-protein signalling (RGS) are a family of proteins that interact with G-proteins to regulate negatively G-protein coupled receptor (GPCR) signalling. In addition to a conserved core domain that is necessary and sufficient for their GTPase activating protein (GAP) like activity, RGSs possess N- and C-terminal motifs that confer distinct functional differences. In order to identify the role of the non-RGS region of human RGS1, we have characterized a series of fusions between RGS1 and GFP in a yeast mutant lacking the RGS containing SST2 gene. Using both halo assays as well as a GPCR responsive FUS1-LacZ reporter gene, we demonstrate that a RGS1-GFP fusion inhibits GPCR signalling in yeast while GFP fusions containing either the N-terminus non RGS sequence of RGS1(1-68) or the sequence containing the RGS box of RGS1(68-197) produce proteins that retain RGS1 activity. These results suggest that both the N-terminal and the RGS box of RGS1 function to inhibit signalling. Analysis of a series of mutants spanning the entire N-terminal non-RGS region of RGS1 produced by conservative segment exchange (CSE) mutagenesis showed little loss of function in yeast. This suggests that the overall structure of the N-terminal region of RGS1 rather than specific motifs or residues is required for its function.
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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-Binding Protein Regulators,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pheromones,
http://linkedlifedata.com/resource/pubmed/chemical/SST2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0898-6568
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
413-21
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12618216-Amino Acid Sequence,
pubmed-meshheading:12618216-GTP-Binding Protein Regulators,
pubmed-meshheading:12618216-GTP-Binding Proteins,
pubmed-meshheading:12618216-GTPase-Activating Proteins,
pubmed-meshheading:12618216-Genes, Reporter,
pubmed-meshheading:12618216-Humans,
pubmed-meshheading:12618216-Molecular Sequence Data,
pubmed-meshheading:12618216-Mutation,
pubmed-meshheading:12618216-Pheromones,
pubmed-meshheading:12618216-Plasmids,
pubmed-meshheading:12618216-Saccharomyces cerevisiae,
pubmed-meshheading:12618216-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12618216-Signal Transduction
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pubmed:year |
2003
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pubmed:articleTitle |
The N-terminal non-RGS domain of human regulator of G-protein signalling 1 contributes to its ability to inhibit pheromone receptor signalling in yeast.
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pubmed:affiliation |
Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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