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J Biol Chem, Vol. 275, Issue 5, 3397-3402, February 4, 2000
From the Regulators of G protein signaling (RGS) stimulate
the GTPase activity of G protein G
Co-expression of G
5 Enhances the Function of Two G
Subunit-like Domain-containing Regulators of G Protein Signaling
Proteins*
§,§,, and
Division of Biology, California Institute of
Technology, Pasadena, California 91125 and ¶ Verna and Marrs
McLean Department of Biochemistry, Baylor College of Medicine,
Houston, Texas 77030
subunits and probably play
additional roles. Some RGS proteins contain a G
subunit-like (GGL)
domain, which mediates a specific interaction with G
5. The role of
such interactions in RGS function is unclear. RGS proteins can
accelerate the kinetics of coupling of G protein-coupled receptors to
G-protein-gated inwardly rectifying K+ (GIRK)
channels. Therefore, we coupled m2-muscarinic acetylcholine receptors
to GIRK channels in Xenopus oocytes to evaluate the effect
of G5 on RGS function. Co-expression of either RGS7 or RGS9 modestly
accelerated GIRK channel kinetics. When G5 was co-expressed with
either RGS7 or RGS9, the acceleration of GIRK channel kinetics was
strongly increased over that produced by RGS7 or RGS9 alone. RGS
function was not enhanced by co-expression of G1, and co-expression
of G5 alone had no effect on GIRK channel kinetics. G5 did not
modulate the function either of RGS4, an RGS protein that lacks a GGL
domain, or of a functional RGS7 construct in which the GGL domain was
omitted. Enhancement of RGS7 function by G5 was not a consequence of
an increase in the amount of plasma membrane or cytosolic RGS7 protein.
*
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.
To whom correspondence should be addressed: Division of
Biology, MC 156-29, California Institute of Technology, Pasadena, CA
91125. Tel.: 626-395-4946; Fax: 626-564-8709; E-mail:
lester@caltech.edu.
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