Advertisement

Recoverin And Rhodopsin Kinase

  • Ching-Kang Jason Chen
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 514)

Abstract

The majority of proteins involved in vertebrate phototransduction are expressed specifically in photoreceptors. Recoverin and rhodopsin kinase are expressed primarily in retinal photoreceptors and they interact with each other in a Ca2+-depen dent manner. This Ca2+-dependent interaction has been studied extensively in vitro. Experiments utilizing animal models and electrophysiological approaches have started to provide important insight regarding its in vivo function. Recoverin can be viewed as a negative regulator of rhodopsin kinase in vertebrate phototransduction. This interaction imparts a negative feedback loop at the receptor level and may play an important role in light adaptation and in recovery.

Keywords

Visual Pigment Cone Photoreceptor Retinal Photoreceptor Congenital Stationary Night Blindness Rhodopsin Kinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Burns ME, Baylor DA. Activation, deactivation, and adaptation in vertebrate photoreceptor cells. Annu Rev Neurosci 2001; 24:779–805.PubMedCrossRefGoogle Scholar
  2. 2.
    Chen CK, Burns ME et al. Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. Proc Natl Acad Sci USA 1999; 96(7):3718–3722.PubMedCrossRefGoogle Scholar
  3. 3.
    Lyubarsky AL, Chen C, Simon MI et al. Mice lacking G-protein receptor kinase 1 have profoundly slowed recovery of cone-driven retinal responses. J Neurosci 2000; 20(6):2209–2217.PubMedGoogle Scholar
  4. 4.
    Xu J, Dodd RL, Makino CL et al. Prolonged photoresponses in transgenic mouse rods lacking arrestin. Nature 1997; 389(6650):505–509.PubMedCrossRefGoogle Scholar
  5. 5.
    Wilden U, Hall SW, Kuhn H. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci USA 1986; 83(5):1174–1178.PubMedCrossRefGoogle Scholar
  6. 6.
    Chen CK, Inglese J, Lefkowitz RI et al. Ca(2+)-dependent interaction of recoverin with rhodopsin kinase. J Biol Chem 1995; 270(30):18060–18066.PubMedCrossRefGoogle Scholar
  7. 7.
    Klenchin VA, Calvert PD, Bownds MD. Inhibition of rhodopsin kinase by recoverin. Further evidence for a negative feedback system in phototransduction. J Biol Chem 1995; 270(27):16147–16152.PubMedCrossRefGoogle Scholar
  8. 8.
    Sato N, Kawamura S. Molecular mechanism of S-modulin action: binding target and effect of ATP. J Biochem (Tokyo) 1997; 122(6):1139–1145.CrossRefGoogle Scholar
  9. 9.
    Gorodovikova EN, Senin ti, and Philippov PP. Calcium-sensitive control of rhodopsin phosphorylation in the reconstituted system consisting of photoreceptor membranes, rhodopsin kinase and recoverin. FEBS Lett 1994; 353(2):171–172.PubMedCrossRefGoogle Scholar
  10. 10.
    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(5196):374–377.PubMedCrossRefGoogle Scholar
  11. 11.
    Mendez A., Burns ME, Roca A et al. Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites. Neuron 2000; 28(1):153–164.PubMedCrossRefGoogle Scholar
  12. 12.
    Cideciyan AV, Zhao X, Nielsen L et al. Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man. Proc Natl Acad Sci USA 1998; 95(1):328–333.PubMedCrossRefGoogle Scholar
  13. 13.
    Yamamoto S, Sippel KC, Berson EL et al. Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. Nat Genet 1997; 15(2):175–178.PubMedCrossRefGoogle Scholar
  14. 14.
    Yamada T, Matsumoto M, Kadoi C et al. 1147 del A mutation in the arrestin gene in Japanese patients with Oguchi disease. Ophthalmic Genet 1999; 20(2):117–120.PubMedCrossRefGoogle Scholar
  15. 15.
    Dryja TP. Molecular genetics of Oguchi disease, fundus albipunctatus, and other forms of stationary night blindness: LVII Edward Jackson Memorial Lecture. Am J Ophthalmol 2000; 130(5):547–563.PubMedCrossRefGoogle Scholar
  16. 16.
    Zhao X, Huang J, Khani SC et al. Molecular forms of human rhodopsin kinase (GRKI). J Biol Chem 1998; 273(9):5124–5131.PubMedCrossRefGoogle Scholar
  17. 17.
    Weiss ER, Ducceschi MH, Horner TJ et al. Species-specific differences in expression of Gprotein-coupled receptor kinase (GRK) 7 and GRKI in mammalian cone photoreceptor cells: implications for cone cell phototransduction. J Neurosci 2001; 21(23):9175–9184.PubMedGoogle Scholar
  18. 18.
    Chen C-K, Zhang K, Church-Kopish J et al. Characterization of human GRK7 as a potential cone opsin kinase. Molecular Vision 2001; 7:305–313.PubMedGoogle Scholar
  19. 19.
    Dizhoor AM, Ray S, Kumar S et al. Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase. Science 1991; 251(4996):915–918.PubMedCrossRefGoogle Scholar
  20. 20.
    Dizhoor AM, Ericsson LH, Johnson RS et al. The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids. J Biol Chem 1992;. 267(23):16033–16036.PubMedGoogle Scholar
  21. 21.
    Dizhoor AM, Chen CK, Olshevskaya E et al. Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction. Science 1993; 259(5096):829–832.PubMedCrossRefGoogle Scholar
  22. 22.
    Zozulya S, Stryer L. Calcium-myristoyl protein switch. Proc Nat] Acad Sci USA 1992; 89(23):11569–11573.CrossRefGoogle Scholar
  23. 23.
    Ames JB, Ishima R, Tanaka T et al. Molecular mechanics of calcium-myristoyl switches. Nature 1997; 389(6647):198–202.PubMedCrossRefGoogle Scholar
  24. 24.
    Ames JB, Porumb T, Tanaka T et al. Amino-terminal myristoylation induces cooperative calcium binding to recoverin. J Biol Chem 1995; 270(9):4526–4533.PubMedCrossRefGoogle Scholar
  25. 25.
    Milam AH, Dacey DM, Dizhoor AM. Recoverin immunoreactivity in mammalian cone bipolar cells. Vis Neurosci 1993; 10(1):1–12.PubMedCrossRefGoogle Scholar
  26. 26.
    Hurley JB, Dizhoor AM, Ray S et al. Recoverin’s role: conclusion withdrawn. Science 1993; 260(5109):40.CrossRefGoogle Scholar
  27. 27.
    Dizhoor AM, Olshevskaya EV, Henzel WJ et al. Cloning, sequencing, and expression of a 24-kDa Ca(2+)-binding protein activating photoreceptor guanylyl cyclase. J Biol Chem 1995; 270(42):25200–25206.PubMedCrossRefGoogle Scholar
  28. 28.
    Palczewski K, Subbaraya I, Gorczyca WA et al. Molecular cloning and characterization of retinal photoreceptor guanylyl cyclase-activating protein. Neuron 1994; 13(2):395–404.PubMedCrossRefGoogle Scholar
  29. 29.
    Gorczyca WA, Polans AS, Surgucheva IG et al. Guanylyl cyclase activating protein. A calcium-sensitive regulator of phototransduction. J Biol Chem 1995; 270(37):22029–22036.PubMedCrossRefGoogle Scholar
  30. 30.
    Kawamura S, Murakami M. Calcium-dependent regulation of cyclic GMP phosphodiesterase by a protein from frog retinal rods. Nature 1991; 349(6308):420–423.PubMedCrossRefGoogle Scholar
  31. 31.
    Kawamura S. Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature 1993. 362(6423):855–857.PubMedCrossRefGoogle Scholar
  32. 32.
    Kawamura S, Hisatomi O, Kayada S et al. Recoverin has S-modulin activity in frog rods. J Biol Chem 1993; 268(20):14579–14582.PubMedGoogle Scholar
  33. 33.
    Polans AS, Buczylko 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(5):981–989.PubMedCrossRefGoogle Scholar
  34. 34.
    Chen CK, Hurley JB. Purification of rhodopsin kinase by recoverin affinity chromatography. Methods Enzymol 2000; 315:404–410.PubMedCrossRefGoogle Scholar
  35. 35.
    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; 10(3):23–531.CrossRefGoogle Scholar
  36. 36.
    Erickson MA, Lagnado L, Zozulya S et al. The effect of recombinant recoverin on the photoresponse of truncated rod photoreceptors. Proc Nati Acad Sci USA 1998; 95(11):6474–6479.CrossRefGoogle Scholar
  37. 37.
    Dodd RL, Makino CL, Chen J et al. Visual transduction in transgenic mouse rods lacking recoverin. Invest Ophthalmol Vis Sci 1995; 36:S641.Google Scholar
  38. 38.
    Hurley JB, Chen J. Evaluation of the contributions of recoverin and GCAPs to rod photoreceptor light adaptation and recovery to the dark state. Prog Brain Res 2001; 131:395–405.PubMedCrossRefGoogle Scholar
  39. 39.
    Otto-Bruc AE, Fariss RN, Van Hooser JP, Palczewski K. Phosphorylation of photolyzed rhodopsin is calcium-insensitive in retina permeabilized by alpha-toxin. Proc Natl Acad Sci USA 1998; 95(25):15014–15019.PubMedCrossRefGoogle Scholar
  40. 40.
    Kilbride P, Ebrey TG. Light-initiated changes of cyclic guanosine monophosphate levels in the frog retina measured with quick-freezing techniques. J Gen Physiol 1979; 74(3):415–426.PubMedCrossRefGoogle Scholar
  41. 41.
    Kennedy MJ, Lee KA, Niemi GA et al. Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation. Neuron 2001. 31(1):87–101.PubMedCrossRefGoogle Scholar
  42. 42.
    Levay K, Satpaev DK, Pronin AN et al. Localization of the sites for Ca2+-binding proteins on G protein-coupled receptor kinases. Biochemistry 1998; 37(39):13650–13659.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2002

Authors and Affiliations

  • Ching-Kang Jason Chen
    • 1
  1. 1.Department of Ophthalmology and Visual Sciences and Human GeneticsUniversity of UtahSalt Lake CityUSA

Personalised recommendations