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

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      Publication date:
      Journal: Nature
      Keywords: 3',5'-Cyclic-GMP Phosphodiesterases, metabolism, Animals, Cyclic Nucleotide Phosphodiesterases, Type 6, GTP Phosphohydrolases, Guanosine Triphosphate, Hydrolysis, Mice, Mice, Inbred Strains, Mice, Knockout, Mice, Transgenic, RGS Proteins, genetics, physiology, Retinal Rod Photoreceptor Cells, Rod Cell Outer Segment, Transducin, Vision, Ocular

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          Abstract

          Timely deactivation of the alpha-subunit of the rod G-protein transducin (Galphat) is essential for the temporal resolution of rod vision. Regulators of G-protein signalling (RGS) proteins accelerate hydrolysis of GTP by the alpha-subunits of heterotrimeric G proteins in vitro. Several retinal RGS proteins can act in vitro as GTPase accelerating proteins (GAP) for Galphat. Recent reconstitution experiments indicate that one of these, RGS9-1, may account for much of the Galphat GAP activity in rod outer segments (ROS). Here we report that ROS membranes from mice lacking RGS9-1 hydrolyse GTP more slowly than ROS membranes from control mice. The Gbeta5-L protein that forms a complex with RGS9-1 was absent from RGS9-/- retinas, although Gbeta5-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 Gbeta5-L, is essential for acceleration of hydrolysis of GTP by Galphat and for normal recovery of the photoresponse.

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          A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors.

          Meredith Pugh, Damon G. Lamb (1992)
          1. We have undertaken a theoretical analysis of the steps contributing to the phototransduction cascade in vertebrate photoreceptors. We have explicitly considered only the activation steps, i.e. we have not dealt with the inactivation reactions. 2. From the theoretical analysis we conclude that a single photoisomerization leads to activation of the phosphodiesterase (PDE) with a time course which approximates a delayed ramp; the delay is contributed by several short first-order delay stages. 3. We derive a method for extracting the time course of PDE activation from the measured electrical response, and we apply this method to recordings of the photoresponse from salamander rods. The results confirm the prediction that the time course of PDE activation is a delayed ramp, with slope proportional to light intensity; the initial delay is about 10-20 ms. 4. We derive approximate analytical solutions for the electrical response of the photoreceptor to light, both for bright flashes (isotropic conditions) and for single photons (involving longitudinal diffusion of cyclic GMP in the outer segment). The response to a brief flash is predicted to follow a delayed Gaussian function of time, i.e. after an initial short delay the response should begin rising in proportion to t2. Further, the response-intensity relation is predicted to obey an exponential saturation. 5. These predictions are compared with experiment, and it is shown that the rising phase of the flash response is accurately described over a very wide range of intensities. We conclude that the model provides a comprehensive description of the activation steps of phototransduction at a molecular level.
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            Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase.

            Jeffrey Burns, Rebecca M. C. Spencer, Denis A. Baylor … (1999)
            Phosphorylation is thought to be an essential first step in the prompt deactivation of photoexcited rhodopsin. In vitro, the phosphorylation can be catalyzed either by rhodopsin kinase (RK) or by protein kinase C (PKC). To investigate the specific role of RK, we inactivated both alleles of the RK gene in mice. This eliminated the light-dependent phosphorylation of rhodopsin and caused the single-photon response to become larger and longer lasting than normal. These results demonstrate that RK is required for normal rhodopsin deactivation. When the photon responses of RK-/- rods did finally turn off, they did so abruptly and stochastically, revealing a first-order backup mechanism for rhodopsin deactivation. The rod outer segments of RK-/- mice raised in 12-hr cyclic illumination were 50% shorter than those of normal (RK+/+) rods or rods from RK-/- mice raised in constant darkness. One day of constant light caused the rods in the RK-/- mouse retina to undergo apoptotic degeneration. Mice lacking RK provide a valuable model for the study of Oguchi disease, a human RK deficiency that causes congenital stationary night blindness.
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              Prolonged photoresponses in transgenic mouse rods lacking arrestin.

              R. Dodd, C Makino, D Baylor … (1997)
              Arrestins are soluble cytoplasmic proteins that bind to G-protein-coupled receptors, thus switching off activation of the G protein and terminating the signalling pathway that triggers the cellular response. Although visual arrestin has been shown to quench the catalytic activity of photoexcited, phosphorylated rhodopsin in a reconstituted system, its role in the intact rod cell remains unclear because phosphorylation alone reduces the catalytic activity of rhodopsin. Here we have recorded photocurrents of rods from transgenic mice in which one or both copies of the arrestin gene were disrupted. Photoresponses were unaffected when arrestin expression was halved, indicating that arrestin binding is not rate limiting for recovery of the rod photoresponse, as it is in Drosophila. With arrestin absent, the flash response displayed a rapid partial recovery followed by a prolonged final phase. This behaviour indicates that an arrestin-independent mechanism initiates the quench of rhodopsin's catalytic activity and that arrestin completes the quench. The intensity dependence of the photoresponse in rods lacking arrestin further suggests that, although arrestin is required for normal signal termination, it does not participate directly in light adaptation.
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                Author and article information

                Journal
                PubMed ID:: 10676965
                DOI:: 10.1038/35000601

                ScienceOpen disciplines: Chemistry
                Keywords: 3',5'-Cyclic-GMP Phosphodiesterases,metabolism,Animals,Cyclic Nucleotide Phosphodiesterases, Type 6,GTP Phosphohydrolases,Guanosine Triphosphate,Hydrolysis,Mice,Mice, Inbred Strains,Mice, Knockout,Mice, Transgenic,RGS Proteins,genetics,physiology,Retinal Rod Photoreceptor Cells,Rod Cell Outer Segment,Transducin,Vision, Ocular
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                ScienceOpen disciplines: Chemistry
                Keywords: 3',5'-Cyclic-GMP Phosphodiesterases, metabolism, Animals, Cyclic Nucleotide Phosphodiesterases, Type 6, GTP Phosphohydrolases, Guanosine Triphosphate, Hydrolysis, Mice, Mice, Inbred Strains, Mice, Knockout, Mice, Transgenic, RGS Proteins, genetics, physiology, Retinal Rod Photoreceptor Cells, Rod Cell Outer Segment, Transducin, Vision, Ocular

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