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(Received for publication, January 21, 1997, and in revised form, March 18, 1997)
From the Ernest Gallo Clinic and Research Center, Department of
Neurology, University of California at San Francisco,
San Francisco, California 94110
Phosducin-like protein (PhLP), a widely expressed
ethanol-responsive gene (Miles, M. F., Barhite, S., Sganga, M., and
Elliott, M. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 10831-10835), is a homologue of phosducin, a known major regulator of
G
Volume 272, Number 19,
Issue of May 9, 1997
pp. 12253-12256
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
Subunits
signaling in retina and pineal gland. However, although
phosducin has a well characterized role in retinal phototransduction,
function of the PhLP remains unclear. In this study we examine the
ability of PhLP to bind G dimer in vitro and in
vivo. Using PhLP glutathione S-transferase fusion
proteins, we show that PhLP directly binds G in
vitro. Studies with a series of truncated PhLP fusion proteins indicate independent binding of G to both the amino- and
C-terminal halves of PhLP. Protein-protein interactions between G
and PhLP are inhibited by the 
subunit of Go and
Gi3, suggesting that PhLP can bind only free G.
Finally, we show that PhLP complexes, at least partially, with G
in vivo. Following overexpression of epitope-tagged PhLP
together with G12 proteins in COS-7
cells, a PhLP-G complex is co-immunoprecipitated by monoclonal
antibody directed against the epitope tag. Similarly, polyclonal
anti-PhLP antibody co-precipitates endogenous PhLP and G proteins
from NG108-15 cell lysates. These data are consistent with the
hypothesis that PhLP is a widely expressed modulator of G
function. Furthermore, because alternate forms of the PhLP transcript
are expressed, there may be functional implications for the existence
of two G-binding domains on PhLP.
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