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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-4-4
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pubmed:abstractText |
Starving Dictyostelium discoideum cells monitor the local density of other starving cells by simultaneously secreting and sensing CMF. CMF regulates signal transduction through the chemoattractant cAMP receptor, cAR1. cAR1 activates a heterotrimeric G protein by stimulating G alpha 2 to release GDP and bind GTP. We show here that the rate of cAMP-stimulated GTP hydrolysis in membranes from cells exposed to CMF is roughly 4 times slower than in membranes from untreated cells, even though the rate of GTP binding is the same. This hydrolysis is abolished in cells lacking G alpha 2. Our data thus suggest that CMF regulates cAMP signal transduction in part by prolonging the lifetime of the G alpha 2-GTP complex.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
404
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
100-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9074646-Animals,
pubmed-meshheading:9074646-Cell Adhesion Molecules,
pubmed-meshheading:9074646-Chemokines,
pubmed-meshheading:9074646-Cyclic AMP,
pubmed-meshheading:9074646-Dictyostelium,
pubmed-meshheading:9074646-GTP-Binding Proteins,
pubmed-meshheading:9074646-Guanosine Triphosphate,
pubmed-meshheading:9074646-Hydrolysis,
pubmed-meshheading:9074646-Protein Conformation,
pubmed-meshheading:9074646-Protozoan Proteins,
pubmed-meshheading:9074646-Signal Transduction
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pubmed:year |
1997
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pubmed:articleTitle |
A cell-density sensing factor regulates the lifetime of a chemoattractant-induced G alpha-GTP conformation.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry and Cell Biology, Houston, TX 77251-1892, 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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