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J Biol Chem, Vol. 275, Issue 2, 921-929, January 14, 2000
From the In neuronal and atrial tissue, G protein-gated
inwardly rectifying K+ channels (Kir3.x family) are
responsible for mediating inhibitory postsynaptic potentials and
slowing the heart rate. They are activated by G
The G Protein
Subunit Has a Key Role in Determining the
Specificity of Coupling to, but Not the Activation of, G Protein-gated
Inwardly Rectifying K+ Channels*
,
Centre for Clinical Pharmacology, Department
of Medicine, University College London, Rayne Institute, 5 University
Street, London WC1E 6JJ and the § Division of Biochemistry
and Molecular Biology, University of Glasgow,
Glasgow G12 8QQ, United Kingdom
dimers released
in response to the stimulation of receptors coupled to inhibitory G
proteins of the Gi/o family but not receptors coupled to
the stimulatory G protein Gs. We have used biochemical, electrophysiological, and molecular biology techniques to examine this
specificity of channel activation. In this study we have succeeded in
reconstituting such specificity in an heterologous expression system
stably expressing a cloned counterpart of the neuronal channel (Kir3.1
and Kir3.2A heteromultimers). The use of pertussis toxin-resistant G
protein 
subunits and chimeras between Gi1 and
Gs indicate a central role for the G protein subunits
in determining receptor specificity of coupling to, but not activation
of, G protein-gated inwardly rectifying K+ channels.
*
This work was supported by the Human Frontiers Science
Program and the Wellcome Trust.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
i1 point
mutants and G should be addressed. E-mail:
gbca32@udcf.gla.ac.uk.
To whom all other correspondence should be addressed. Tel.:
44-171-209-6174; Fax: 44-171-813-2846 or 44-171-209-6212; E-mail: a.tinker@ucl.ac.uk.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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