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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Ching-Kang Chen & Marie E. Burns & Wei He & Theodore G. Wensel & Denis A. Baylor & Melvin I. Simon, 2000. "Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1," Nature, Nature, vol. 403(6769), pages 557-560, February.
    • Handle: RePEc:nat:nature:v:403:y:2000:i:6769:d:10.1038_35000601
    DOI: 10.1038/35000601
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