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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1999-4-15
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pubmed:databankReference |
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pubmed:abstractText |
G protein-coupled receptors are commonly thought to bind their cognate ligands and elicit functional responses primarily as monomeric receptors. In studying the recombinant gamma-aminobutyric acid, type B (GABAB) receptor (gb1a) and a GABAB-like orphan receptor (gb2), we observed that both receptors are functionally inactive when expressed individually in multiple heterologous systems. Characterization of the tissue distribution of each of the receptors by in situ hybridization histochemistry in rat brain revealed co-localization of gb1 and gb2 transcripts in many brain regions, suggesting the hypothesis that gb1 and gb2 may interact in vivo. In three established functional systems (inwardly rectifying K+ channel currents in Xenopus oocytes, melanophore pigment aggregation, and direct cAMP measurements in HEK-293 cells), GABA mediated a functional response in cells coexpressing gb1a and gb2 but not in cells expressing either receptor individually. This GABA activity could be blocked with the GABAB receptor antagonist CGP71872. In COS-7 cells coexpressing gb1a and gb2 receptors, co-immunoprecipitation of gb1a and gb2 receptors was demonstrated, indicating that gb1a and gb2 act as subunits in the formation of a functional GABAB receptor.
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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/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/CGP 71872,
http://linkedlifedata.com/resource/pubmed/chemical/G Protein-Coupled...,
http://linkedlifedata.com/resource/pubmed/chemical/GABA type B receptor, subunit 1,
http://linkedlifedata.com/resource/pubmed/chemical/GABBR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Gabbr2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Organophosphorus Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Inwardly...,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, GABA-B
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:BonnerT ITI,
pubmed-author:ChateauneufAA,
pubmed-author:ClarkJJ,
pubmed-author:CoulombeNN,
pubmed-author:EthierNN,
pubmed-author:EvansJ FJF,
pubmed-author:HebertT ETE,
pubmed-author:JohnsonM PMP,
pubmed-author:KargmanSS,
pubmed-author:KolakowskiL FLFJr,
pubmed-author:LieAA,
pubmed-author:LoG SGS,
pubmed-author:McDonaldTT,
pubmed-author:MezeyEE,
pubmed-author:O'NeillG PGP,
pubmed-author:SullivanRR,
pubmed-author:TsukamotoNN,
pubmed-author:WhitingPP
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7607-10
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pubmed:dateRevised |
2006-6-1
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pubmed:meshHeading |
pubmed-meshheading:10075644-Amino Acid Sequence,
pubmed-meshheading:10075644-Animals,
pubmed-meshheading:10075644-Azides,
pubmed-meshheading:10075644-COS Cells,
pubmed-meshheading:10075644-Dimerization,
pubmed-meshheading:10075644-G Protein-Coupled Inwardly-Rectifying Potassium Channels,
pubmed-meshheading:10075644-Humans,
pubmed-meshheading:10075644-In Situ Hybridization,
pubmed-meshheading:10075644-Mice,
pubmed-meshheading:10075644-Molecular Sequence Data,
pubmed-meshheading:10075644-Organophosphorus Compounds,
pubmed-meshheading:10075644-Potassium Channels,
pubmed-meshheading:10075644-Potassium Channels, Inwardly Rectifying,
pubmed-meshheading:10075644-Protein Conformation,
pubmed-meshheading:10075644-RNA, Messenger,
pubmed-meshheading:10075644-Rats,
pubmed-meshheading:10075644-Receptors, GABA-B,
pubmed-meshheading:10075644-Structure-Activity Relationship,
pubmed-meshheading:10075644-Xenopus laevis
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pubmed:year |
1999
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pubmed:articleTitle |
Identification of a GABAB receptor subunit, gb2, required for functional GABAB receptor activity.
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pubmed:affiliation |
Merck Frosst Center for Therapeutic Research, Kirkland, Quebec H9H 3L1, Canada. gordon_ng@merck.com
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pubmed:publicationType |
Journal Article
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