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cGMP-dependent cation channel of retinal rod outer segments

Nature volume 326, pages 600–603 (1987)Cite this article

Abstract

Light-modulated cytoplasmic cGMP simultaneously controls plasma membrane Na+ conductance in visual excitation and Ca2+ entry into rods by direct interaction with the cation channel1–3. Cytoplasmic Ca2+ in turn may set operating points and contribute to the dynamics of several enzymes that regulate cGMP levels in the dark4–6, recovery from excitation and receptor adaptation or down regulation7. Similar channels may couple electrical activity to internal nucleotide metabolism in other tissues. We here report the identification, partial purification and behaviour after reconstitution of a protein of relative molecular mass 39,000 (Mr 39K) present in both disk and plasma membranes from bovine rod outer segments that mediates these cGMP-dependent cation fluxes. Its cGMP agonist specificity, kinetic cooperativity, ionic selectivity, membrane density and other features closely match the properties of the visual cGMP-dependent conductance inferred from elec-trophysiological measurements1,2,8,9.

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Authors and Affiliations

  1. Departments of Biochemistry and Biophysics and Anatomy, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania, 19104, USA

    Diane Matesic & Paul A. Liebman

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  1. Diane Matesic
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  2. Paul A. Liebman
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Matesic, D., Liebman, P. cGMP-dependent cation channel of retinal rod outer segments. Nature 326, 600–603 (1987). https://doi.org/10.1038/326600a0

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