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J. Biol. Chem., Vol. 275, Issue 42, 32716-32720, October 20, 2000
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From the Department of Ophthalmology, Harvard Medical School,
Massachusetts Eye and Ear Infirmary, Boston Massachusetts 02114
The photoreceptor-specific G protein transducin
acts as a molecular switch, stimulating the activity of its downstream
effector in its GTP-bound form and inactivating the effector
upon GTP hydrolysis. This activity makes the rate of transducin GTPase
an essential factor in determining the duration of photoresponse in
vertebrate rods and cones. In photoreceptors, the slow intrinsic rate
of transducin GTPase is accelerated by the complex of the ninth member of the regulators of G protein
signaling family with the long splice variant
of type 5 G protein
The Effector Enzyme Regulates the Duration of G Protein Signaling
in Vertebrate Photoreceptors by Increasing the Affinity between
Transducin and RGS Protein*
subunit
(RGS9·G5L). However, physiologically rapid GTPase is
observed only when transducin forms a complex with its effector, the
subunit of cGMP phosphodiesterase (PDE). In this study, we
addressed the mechanism by which PDE regulates the rate of
transducin GTPase. We found that RGS9·G5L alone has a significant
ability to activate transducin GTPase, but its affinity for transducin
is low. PDE acts by enhancing the affinity between activated
transducin and RGS9·G5L by more than 15-fold, which is evident
both from kinetic measurements of transducin GTPase rate and from
protein binding assays with immobilized transducin. Furthermore, our
data indicate that a single RGS9·G5L molecule is capable of
accelerating the GTPase activity of ~100 transducin molecules/s. This
rate is faster than the rates reported previously for any RGS protein
and is sufficient for timely photoreceptor recovery in both rod and
cone photoreceptors.
*
This work was supported by National Institutes of Health
Grant EY-12859 and a grant from the Massachusetts Lions Eye Research Fund (to V. Y. A.).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.
Recipient of the Jules and Doris Stein Professorship from Research
to Prevent Blindness Inc. To whom correspondence should be addressed:
Howe Laboratory of Ophthalmology, Harvard Medical School/MEEI, 243 Charles St., Boston, MA 02114; Tel.: 617-573-4371; Fax: 617-573-4290;
E-mail: vadim_arshavsky@meei.harvard.edu.
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