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.
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Acknowledgements
We thank members of the Caltech Transgenic Core Facility for their technical support, and R. Lefkowitz, J. Hurley and H. Jurgen-Fuller for antibodies. This work was supported by grants from the NIH.
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Chen, CK., Burns, M., He, W. et al. Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1. Nature 403, 557–560 (2000). https://doi.org/10.1038/35000601
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DOI: https://doi.org/10.1038/35000601
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