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rdf:type |
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lifeskim:mentions |
umls-concept:C0001455,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0043393,
umls-concept:C0086376,
umls-concept:C0205314,
umls-concept:C0439851,
umls-concept:C0679622,
umls-concept:C1335616,
umls-concept:C1425268,
umls-concept:C1552596,
umls-concept:C1704259,
umls-concept:C1704735,
umls-concept:C1705987,
umls-concept:C1710082,
umls-concept:C1947931
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pubmed:issue |
20
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pubmed:dateCreated |
1999-12-6
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pubmed:abstractText |
We have characterized a novel member of the recently identified family of regulators of heterotrimeric G protein signalling (RGS) in the yeast Saccharomyces cerevisiae. The YOR107w/RGS2 gene was isolated as a multi-copy suppressor of glucose-induced loss of heat resistance in stationary phase cells. The N-terminal half of the Rgs2 protein consists of a typical RGS domain. Deletion and overexpression of Rgs2, respectively, enhances and reduces glucose-induced accumulation of cAMP. Overexpression of RGS2 generates phenotypes consistent with low activity of cAMP-dependent protein kinase A (PKA), such as enhanced accumulation of trehalose and glycogen, enhanced heat resistance and elevated expression of STRE-controlled genes. Deletion of RGS2 causes opposite phenotypes. We demonstrate that Rgs2 functions as a negative regulator of glucose-induced cAMP signalling through direct GTPase activation of the Gs-alpha protein Gpa2. Rgs2 and Gpa2 constitute the second cognate RGS-G-alpha protein pair identified in yeast, in addition to the mating pheromone pathway regulators Sst2 and Gpa1. Moreover, Rgs2 and Sst2 exert specific, non-overlapping functions, and deletion mutants in Rgs2 and Sst2 are complemented to some extent by different mammalian RGS proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GPA1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Gpa2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rgs2 protein, mouse,
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 |
Oct
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5577-91
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10523302-Amino Acid Sequence,
pubmed-meshheading:10523302-Animals,
pubmed-meshheading:10523302-Cyclic AMP,
pubmed-meshheading:10523302-Down-Regulation,
pubmed-meshheading:10523302-Fungal Proteins,
pubmed-meshheading:10523302-GTP-Binding Protein alpha Subunits,
pubmed-meshheading:10523302-GTP-Binding Protein alpha Subunits, Gq-G11,
pubmed-meshheading:10523302-GTP-Binding Proteins,
pubmed-meshheading:10523302-GTPase-Activating Proteins,
pubmed-meshheading:10523302-Gene Deletion,
pubmed-meshheading:10523302-Gene Expression,
pubmed-meshheading:10523302-Genes, Fungal,
pubmed-meshheading:10523302-Genetic Complementation Test,
pubmed-meshheading:10523302-Glucose,
pubmed-meshheading:10523302-Guanosine Triphosphate,
pubmed-meshheading:10523302-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:10523302-Hydrolysis,
pubmed-meshheading:10523302-Mice,
pubmed-meshheading:10523302-Molecular Sequence Data,
pubmed-meshheading:10523302-Phenotype,
pubmed-meshheading:10523302-RGS Proteins,
pubmed-meshheading:10523302-Saccharomyces cerevisiae,
pubmed-meshheading:10523302-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10523302-Sequence Homology, Amino Acid,
pubmed-meshheading:10523302-Signal Transduction
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pubmed:year |
1999
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pubmed:articleTitle |
A novel regulator of G protein signalling in yeast, Rgs2, downregulates glucose-activation of the cAMP pathway through direct inhibition of Gpa2.
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pubmed:affiliation |
Laboratorium voor Moleculaire Celbiologie, Instituut voor Plantkunde en Microbiologie, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven-Heverlee, Flanders, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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