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(Received for publication, September 19, 1996, and in revised form, November 4, 1996)
From the Department of Pharmacology and the
§ Departments of Medicine and Pathology, University of
Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
The selectivity in coupling of various receptors
to GTP-binding regulatory proteins (G proteins) was examined directly
by a novel assay entailing the use of proteins overexpressed in
Spodoptera frugiperda (Sf9) cells. Activation of G proteins
was monitored in membranes prepared from Sf9 cells co-expressing
selected pairs of receptors and G proteins (i.e.
Volume 272, Number 4,
Issue of January 24, 1997
pp. 2223-2229
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
A DIRECT EVALUATION OF SELECTIVITY IN RECEPTOR·G PROTEIN
COUPLING
,
1, and 
2 subunits). Membranes were
incubated with [35S]guanosine
5
-(3-O-thio)triphosphate (GTPS) ± an agonist, and the
amount of radiolabel bound to the subunit was quantitated following
immunoprecipitation. When expressed without receptor (but with
12), the G protein subunits
z, 12, and 13 did not bind
appreciable levels of [35S]GTPS, consistent with a
minimal level of GDP/[35S]GTPS exchange. In contrast,
the subunits s and q bound measurable levels of the nucleotide. Co-expression of the
5-hydroxytryptamine1A (5-HT1A) receptor
promoted binding of [35S]GTPS to z but
not to 12, 13, or s.
Binding to z was enhanced by inclusion of serotonin in
the assay. Agonist activation of both thrombin and neurokinin-1
receptors promoted a modest increase in [35S]GTPS
binding to z and more robust increases in binding to q, 12, and 13. Binding of
[35S]GTPS to s was strongly enhanced
only by the activated 1-adrenergic receptor. Our data
identify interactions of receptors and G proteins directly, without
resort to measurements of effector activity, confirm the coupling of
the 5-HT1A receptor to Gz and extend the list
of receptors that interact with this unique G protein to the receptors
for thrombin and substance P, imply constitutive activity for the
5-HT1A receptor, and demonstrate for the first time that
the cloned receptors for thrombin and substance P activate G12 and G13.
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