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J Biol Chem, Vol. 274, Issue 12, 7607-7610, March 19, 1999
From a Merck Frosst Center for Therapeutic Research,
Kirkland, Quebec H9H 3L1, Canada, the i Merck Sharp & Dohme
Research Laboratories, Terlings Park, Harlow, Essex CM20 2QR, United
Kingdom, g Banyu Pharmaceutical Co., Ltd., Tsukuba-shi,
Ibaraki-ken 300-2611, Japan, h Merck & Co., Inc., West Point,
Pennsylvania, 19486, f Montreal Heart Institute, Montreal,
Quebec H1T 1C8, Canada, d National Institutes of Mental Health, G protein-coupled receptors are
commonly thought to bind their cognate ligands and elicit functional
responses primarily as monomeric receptors. In studying the recombinant
-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.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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