Abstract
S-Modulin is a CaZ+-binding protein found in frog rod photoreceptorst,2and its bovine homologue is known as recoverin3’4. In the CaZ+-bound form, S-modulin inhibits rhodopsin phosphorylation5through inhibition of rhodopsin kinase.6-9Because rhodopsin phosphorylation is the quench mechanism of light-activated rhodopsin (R*)10,11the inhibition of the phosphorylation by S-modulin probably contributes to increase the lifetime of R* to result in sustained hydrolysis of cGMP5. The CaZ+concentration decreases in the light in vertebrate photoreceptors12-14and this decrease is essential for light-adaptation.15,16Thus, S-modulin is expected to regulate the lifetime of R* and thereby regulate the extent and the time course of hydrolysis of cGMP depending on the intensity of background light. With this mechanism, S-modulin is believed to regulate the waveform of a photoresponse and the efficiency of the light in the generation of a photoresponse.
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References
Kawamura S, Murakami M. Calcium-dependent regulation of cyclic GMP phosphodiesterase by a protein from frog retinal rods. Nature 1991; 349:420–423.
Kawamura S. Light-sensitivity modulating protein in frog rods. Photochem Photobiol 1992; 56:1173–1180.
Dizhoor AM, Ray S, Kumar S et al. Recoverin: a calcium sensitive activator of retinal guanylate cyclase. Science 1991; 251:915–918.
Kawamura S, Hisatomi 0, Kayada S et al. Recoverin has S-modulin activity in frog rods. J Biol Chem 1993; 268:14579–14582.
Kawamura S. Rhodopsin phosphorylation as a mechanism of cGMP phosphodiesterase regulation by S-modulin. Nature 1993; 362:855–857.
Gorodovikova EN, Philippov PD. The presence of a calcium-sensitive p26-containing complex in bovine retina rod cells. FEBS Lett 1993; 335:277–279.
Chen C-K, Inglese J, Lefkowitz RJ et al. Ca2+-dependent interaction of recoverin with rhodopsin kinase. J Biol Chem 1995; 270:18060–18066.
Klenchin VA, Calvert PD, Bownds MD. Inhibition of rhodopsin kinase by recoverin. J Biol Chem 1995; 270:16147–16152.
Sanada K, Shimizu F, Kameyama K et al. Calcium-bound recoverin targets rhodopsin kinase to membranes to inhibit rhodopsin phosphorylation. FEBS Lett 1996; 384:227–230.
Chen J, Makino CL, Peachey NS et al. Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant. Science 1995; 267:374–377.
Chen CK, Burns ME, Spencer M et al. Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. Proc Natl Acad Sci USA 1999; 96:3718–3722.
McCarthy ST, Younger JP, Owen WG. Dynamic, spatially nonuniform calcium regulation in frog rods exposed to light. J Neurophysiol 1996; 76:1991–2004.
Sampath AP, Matthews HR, Cornwall MC et al. Bleached pigment produces a maintained decrease in outer segment CaZ+in salamander rods. J Gen Physiol 1998; 111:53–64.
Gray-Keller MP, Detwiler PB. The calcium feedback signal in the phototransduction cascade of vertebrate rods. Neuron 1994; 13:849–861.
Matthews HR, Murphy RLW, Fain GL et al. Photoreceptor light adaptation is mediated by cytoplasmic calcium concentration. Nature 1988; 334:67–69.
Nakatani K, Yau KW. 1988 Calcium and light adaptation in retinal rods and cones. Nature 314:69–71.
Kawamura S, Takamatsu K, Kitamura K. Purification and characterization of S-modulin, a calcium-dependent regulator on cGMP phosphodiesterase in frog rod photoreceptors. Biochem Biophys Res Commun 1992; 186:411–417.
Polans AS, Buczytko J, Crabb J et al. A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy. J Cell Biol 1991; 112:981–989.
Kawamura S, Kuwata O, Yamada M et al. Photoreceptor protein s26, a cone homologue of S-modulin in frog retina. J Biol Chem 1996; 271:21359–21364.
Gray-Keller MP, Polans AS, Palczewski K et al. The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods. Neuron 1993; I0:523–531.
Sagoo MS, Lagnado L. G-protein deactivation is rate-limiting for shut-off of the phototransduction cascade. Nature 1997; 389:392–394.
Matthews HR. Actions of CaZ+on an early stage in phototransduction revealed by the dynamic fall in CaZ+concentration during the bright flash response. J Gen Physiol 1997; 109:141–146.
Dodd RL, Makino CL, Chen J et al. Visual transduction in transgenic mouse lacking recoverin. Invest Ophthalmol Vis Sci 1995; 36:S641.
Erickson MA, Lagnado L, Zozulya S et al. The effect of recombinant recoverin on the photoresponse of truncated rod photoreceptors. Proc Natl Acad Sci USA 1998; 95:6474–6479.
Otto-Bruc AE, Fariss RN, Van Hooser JP et al. Phosphorylation of photolyzed rhodopsin is calcium-insensitive in retina permeabilizesd by a-toxin. Proc Natl Acd Sci USA 1998; 95:15014–15019.
Koutalos Y, Yau KW. Regulation of sensitivity in vertebrate rod photoreceptors by calcium. Trends Neurosci 1996; 19:73–81.
Mendez A, Burns ME, Sokal et al. Role of guanylate cyclase-activating proteins (GCAPs) in setting the flash sensitivity of rod photoreceptors. Proc Natl Acad Sci USA 2001; 98:9948–9953.
Sato N, Kawamura S. Molecular mechanism of S-modulin action: Binding target and effect of ATP. J. Biochem 1997; 122:1139–1145.
Tachibanaki S, Nanda K, Sasaki K et al. Amino acid residues of S-modulin responsible for interaction with rhodopsin kinase. J Biol Chem 2000; 275:3313–3319.
Tanaka T, Ames JB, Harvey TS et al. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 1995; 376:444–447
Ames JB, Ishima R, Tanaka T et al. Molecular mechanics of calcium-myristoyl switches. Nature 1997; 389:198–202.
Johnson WC, Palczewski K, Gorczyca WA et al. Calcium binding to recoverin: implications for secondary structure and membrane association. 1997; Biochimica et Biophysica Acta 1997; 1342:164–174.
De Castro E, Nef S, Fiumelli H et al. Regulation of rhodopsin phosphorylation by a family of neuronal calcium sensors. Biochem Biophys Res Commun 1995; 216:133–140.
Yamagata K, Goto K, Kuo CH et al. Visinin: a novel calcium binding protein expressed in retinal cone cells. Neuron 1990; 2:469–476.
Flaherty KM, Zozulya S, Stryer L et al. Three-dimentional structure of recoverin, a calcium sensor in vision. Cell 1993; 75:709–716.
Dizhoor MD, Ericsson LH, Johnson RS et al. The NH2terminus of retinal recoverin is acylated by a small family of fatty acids. J Biol Chem 1992; 267:16033–16036.
Zozulya S, Stryer L. 1992 Calcium-myristoyl switch. Proc Natl Acad Sci USA 89:11569–11573.
Dizhoor AM, Chen CK, Olshevskaya E et al. Role of the acylated amino terminus of recoverin in Cat+-dependent membrane interaction. Science 1993; 259:829–832.
Kawamura S, Cox JA, Nef P. Inhibition of rhodopsin phosphorylation by non-myristoylated recombinant recoverin. Biochem Biophys Res Commun 1994; 203:121–127.
Calvert PD, Klenchin VA, Bownds MD. Rhodopsin kinase inhibition by recoverin. J Biol Chem 1995; 270:24127–24129.
Ames JB, Porumb T, Tanaka T et al. Amino-terminal myristoylation induces cooperative calcium binding to recoverin. J Biol Chem 1995; 270:4526–4533.
Matsuda S, Hisatomi O, Ishino T et al. The role of calcium-binding sites in S-modulin function. J Biol Chem 1998; 273:20223–20227.
Matsuda S, Hisatomi O, TokunagaF.Role of carboxyl-terminal charges on S-modulin membrane affinity and inhibition of rhodopsin phosphorylation. Biochemistry 1999; 38:1310–1315.
Pongs O, Lindemeier J, Zhu XR, et al. Frequenin-a novel calcium-binding protein that modulate synaptic efficacy in the Drosophila nervous system. Neuron 1993; 11:15–28.
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Kawamura, S., Tachibanaki, S. (2002). S-Modulin. In: Baehr, W., Palczewski, K. (eds) Photoreceptors and Calcium. Advances in Experimental Medicine and Biology, vol 514. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0121-3_4
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DOI: https://doi.org/10.1007/978-1-4615-0121-3_4
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