Source:http://linkedlifedata.com/resource/pubmed/id/11234015
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6823
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pubmed:dateCreated |
2001-3-6
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pubmed:abstractText |
The heterotrimeric G-protein Gs couples cell-surface receptors to the activation of adenylyl cyclases and cyclic AMP production (reviewed in refs 1, 2). RGS proteins, which act as GTPase-activating proteins (GAPs) for the G-protein alpha-subunits alpha(i) and alpha(q), lack such activity for alpha(s) (refs 3-6). But several RGS proteins inhibit cAMP production by Gs-linked receptors. Here we report that RGS2 reduces cAMP production by odorant-stimulated olfactory epithelium membranes, in which the alpha(s) family member alpha(olf) links odorant receptors to adenylyl cyclase activation. Unexpectedly, RGS2 reduces odorant-elicited cAMP production, not by acting on alpha(olf) but by inhibiting the activity of adenylyl cyclase type III, the predominant adenylyl cyclase isoform in olfactory neurons. Furthermore, whole-cell voltage clamp recordings of odorant-stimulated olfactory neurons indicate that endogenous RGS2 negatively regulates odorant-evoked intracellular signalling. These results reveal a mechanism for controlling the activities of adenylyl cyclases, which probably contributes to the ability of olfactory neurons to discriminate odours.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine 5'-O-(3-Thiotriphosphate),
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rgs2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/adenylate cyclase 3
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
409
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1051-5
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pubmed:dateRevised |
2010-6-22
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pubmed:meshHeading |
pubmed-meshheading:11234015-Adenylate Cyclase,
pubmed-meshheading:11234015-Animals,
pubmed-meshheading:11234015-Cell Line,
pubmed-meshheading:11234015-Cell Membrane,
pubmed-meshheading:11234015-Cyclic AMP,
pubmed-meshheading:11234015-Enzyme Activation,
pubmed-meshheading:11234015-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:11234015-Isoenzymes,
pubmed-meshheading:11234015-Olfactory Receptor Neurons,
pubmed-meshheading:11234015-Patch-Clamp Techniques,
pubmed-meshheading:11234015-RGS Proteins,
pubmed-meshheading:11234015-Rats,
pubmed-meshheading:11234015-Recombinant Proteins,
pubmed-meshheading:11234015-Signal Transduction,
pubmed-meshheading:11234015-Transfection
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pubmed:year |
2001
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pubmed:articleTitle |
RGS2 regulates signal transduction in olfactory neurons by attenuating activation of adenylyl cyclase III.
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pubmed:affiliation |
Laboratory of Immunoregulation, NIAID, NIH, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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