Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1

Ching-Kang Chen, Marie E. Burns, Wei He, Theodore G. Wensel, Denis A. Baylor and Melvin I. Simon ()
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Ching-Kang Chen: 147-75, California Institute of Technology
Marie E. Burns: Stanford University Medical Center
Wei He: Baylor College of Medicine
Theodore G. Wensel: Baylor College of Medicine
Denis A. Baylor: Stanford University Medical Center
Melvin I. Simon: 147-75, California Institute of Technology

Nature, 2000, vol. 403, issue 6769, 557-560

Abstract: Abstract Timely deactivation of the α-subunit of the rod G-protein transducin (Gαt) is essential for the temporal resolution of rod vision1. Regulators of G-protein signalling (RGS) proteins accelerate hydrolysis of GTP by the α-subunits of heterotrimeric G proteins2,3,4 in vitro. Several retinal RGS proteins can act in vitro as GTPase accelerating proteins (GAP) for Gαt5,6,7,8. Recent reconstitution experiments indicate that one of these, RGS9-1, may account for much of the Gαt GAP activity in rod outer segments (ROS)8,9. Here we report that ROS membranes from mice lacking RGS9-1 hydrolyse GTP more slowly than ROS membranes from control mice. The Gβ5-L protein that forms a complex with RGS9-1 (ref. 10) was absent from RGS9-/- retinas, although Gβ5-L messenger RNA was still present. The flash responses of RGS9-/- rods rose normally, but recovered much more slowly than normal. We conclude that RGS9-1, probably in a complex with Gβ5-L, is essential for acceleration of hydrolysis of GTP by Gαt and for normal recovery of the photoresponse.

Date: 2000
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DOI: 10.1038/35000601

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