Guanylate cyclase-activating proteins and retina disease

Subcellular Biochemistry

Volumn 45, Issue , 2007, Pages 71-91

  Baehr, W ^a   Palczewski, K ^b  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Ca2+ binding protein; Calcium; Cone dystrophy; Dominant cone dystrophy; EF hand motif; Guanylate cyclase (GC); Guanylate cyclase activating proteins (GCAPs); Leber Congenital Amaurosis (LCA); Retina; Rod and cone photoreceptors; Rod outer segments (ROS)

Indexed keywords

GUANYLATE CYCLASE; GUANYLATE CYCLASE ACTIVATOR;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; CALCIUM SIGNALING; ENZYME ACTIVATION; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; MOUSE; MOUSE MUTANT; PATHOPHYSIOLOGY; PHOTORECEPTOR; PHOTOTRANSDUCTION; PHYSIOLOGY; PROTEIN MOTIF; RETINA DISEASE; REVIEW; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CALCIUM SIGNALING; EF HAND MOTIFS; ENZYME ACTIVATION; GUANYLATE CYCLASE; GUANYLATE CYCLASE-ACTIVATING PROTEINS; HUMANS; MICE; MICE, KNOCKOUT; MOLECULAR SEQUENCE DATA; PHOTORECEPTORS; PHOTOTRANSDUCTION; RETINAL DISEASES; SEQUENCE ALIGNMENT;

EID: 38849133024     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4020-6191-2_4     Document Type: Article

References (98)

1. Acland, G.M., Aguirre, G.D., Ray, J., Zhang, Q., Aleman, T.S., Cideciyan, A.V., Pearce-Kelling, S.E., Anand, V., Zeng, Y., Maguire, A.M., Jacobson, S.G., Hauswirth, W.W., and Bennett, J. (2001). Gene therapy restores vision in a canine model of childhood blindness. Nat. Genet. 28: 92-95.
2. Ames, J.B., Dizhoor, A.M., Ikura, M., Palczewski, K., and Stryer, L. (1999). Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. J. Biol. Chem. 274: 19329-19337.
3. Batten, M.L., Imanishi, Y., Tu, D.C., Doan, T., Zhu, L., Pang, J., Glushakova, L., Moise, A.R., Baehr, W., Gelder, R.N., Hauswirth, W.W., Rieke, F., and Palczewski, K. (2005). Pharmacological and rAAV Gene Therapy Rescue of Visual Functions in a Blind Mouse Model of Leber Congenital Amaurosis. PLoS. Med. 2: e333.
4. Baylor, D.A. and Burns, M.E. (1998). Control of rhodopsin activity in vision. Eye 12 (Pt 3b): 521-525.
5. Bennett, J., Maguire, A.M., Cideciyan, A.V., Schnell, M., Glover, E., Anand, V., Aleman, T.S., Chirmule, N., Gupta, A.R., Huang, Y., Gao, G.P., Nyberg, W.C., Tazelaar, J., Hughes, J., Wilson, J.M., and Jacobson, S.G. (1999). Stable transgene expression in rod photoreceptors after recombinant adeno-associated virus-mediated gene transfer to monkey retina. Proc. Natl. Acad. Sci. U. S. A 96: 9920-9925.
6. Bennett, J., Zeng, Y., Bajwa, R., Klatt, L., Li, Y., and Maguire, A.M. (1998). Adenovirus-mediated delivery of rhodopsin-promoted bcl-2 results in a delay in photoreceptor cell death in the rd/rd mouse. Gene Ther. 5: 1156-1164.
7. Bhattacharya, S., Bunick, C.G., and Chazin, W.J. (2004). Target selectivity in EF-hand calcium binding proteins. Biochim. Biophys. Acta 1742: 69-79.
8. Booij, J.C., Florijn, R.J., ten Brink, J.B., Loves, W., Meire, F., van Schooneveld, M.J., de Jong, P.T., and Bergen, A.A. (2005). Identification of mutations in the AIPL1, CRB1, GUCY2D, RPE65, and RPGRIP1 genes in patients with juvenile retinitis pigmentosa. J. Med. Genet. 42: e67.
9. Bourne, Y., Dannenberg, J., Pollmann, V., Marchot, P., and Pongs, O. (2001). Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1). J. Biol. Chem. 276: 11949-11955.
10. Burns, M.E. and Arshavsky, V.Y. (2005). Beyond counting photons: trials and trends in vertebrate visual transduction. Neuron 48: 387-401.
11. Burns, M.E. and Baylor, D.A. (2001). Activation, deactivation, and adaptation in vertebrate photoreceptor cells. Annu. Rev. Neurosci. 24: 779-805.
12. Coleman, J.E., Zhang, Y., Brown, G.A., and Semple-Rowland, S.L. (2004). Cone cell survival and downregulation of GCAP1 protein in the retinas of GC1 knockout mice. Invest Ophthalmol. Vis. Sci 45: 3397-3403.
13. Cuenca, N., Lopez, S., Howes, K., and Kolb, H. (1998). The localization of guanylyl cyclase-activating proteins in the mammalian retina. Invest Ophthalmol. Vis. Sci. 39: 1243-1250.
14. Dizhoor, A.M. (2000). Regulation of cGMP synthesis in photoreceptors: role in signal transduction and congenital diseases of the retina. Cell Signal. 12: 711-719.
15. Dizhoor, A.M., Boikov, S.G., and Olshevskaya, E. (1998). Constitutive activation of photoreceptor guanylate cyclase by Y99C mutant of GCAP-1. J. Biol. Chem. 273: 17311-17314.
16. Downes, S.M., Holder, G.E., Fitzke, F.W., Payne, A.M., Warren, M.J., Bhattacharya, S.S., and Bird, A.C. (2001a). Autosomal dominant cone and cone-rod dystrophy with mutations in the guanylate cyclase activator 1A gene-encoding guanylate cyclase activating protein-1. Arch. Ophthalmol. 119: 96-105.
17. Downes, S.M., Payne, A.M., Kelsell, R.E., Fitzke, F.W., Holder, G.E., Hunt, D.M., Moore, A.T., and Bird, A.C. (2001b). Autosomal dominant cone-rod dystrophy with mutations in the guanylate cyclase 2D gene encoding retinal guanylate cyclase-1. Arch. Ophthalmol. 119: 1667-1673.
18. Duda, T., Goraczniak, R.M., and Sharma, R.K. (1993). The glycine residue of ATP regulatory module in receptor guanylate cyclases that is essential in natriuretic factor signaling. FEBS Lett. 335: 309-314.
19. Duda, T., Goraczniak, R.M., Surgucheva, I., Rudnicka-Nawrot, M., Gorczyca, W.A., Palczewski, K., Sitaramayya, A., Baehr, W., and Sharma, R.K. (1996). Calcium modulation of bovine photoreceptor guanylate cyclase. Biochemistry 35: 8478-8482.
20. Duda, T. and Koch, K.W. (2002). Calcium-modulated membrane guanylate cyclase in synaptic transmission? Mol. Cell Biochem. 230: 107-116.
21. El-Shanti, H., Al-Salem, M., El-Najjar, M., Ajlouni, K., Beck, J., Sheffiled, V.C., and Stone, E.M. (1999). A nonsense mutation in the retinal specific guanylate cyclase gene is the cause of Leber congenital amaurosis in a large inbred kindred from Jordan. J. Med. Genet. 36: 862-865.
22. Falke, J.J., Drake, S.K., Hazard, A.L., and Peerson, O.B. (1994). Molecular tuning of ion binding to calcium signaling proteins. Q. Rev. Biophys. 27: 219-290.
23. Flaherty, K.M., Zozulya, S., Stryer, L., and McKay, D.B. (1993). Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75: 709-716.
24. Fleischman, D., Denisevich, M., Raveed, D., and Pannbacker, R.G. (1980). Association of guanylate cyclase with the axoneme of retinal rods. Biochim. Biophys. Acta 630: 176-186.
25. Gorczyca, W.A., Van Hooser, J.P., and Palczewski, K. (1994). Nucleotide inhibitors and activators of retinal guanylyl cyclase. Biochemistry 33: 3217-3222.
26. Griffith, J.P., Kim, J.L., Kim, E.E., Sintchak, M.D., Thomson, J.A., Fitzgibbon, M.J., Fleming, M.A., Caron, P.R., Hsiao, K., and Navia, M.A. (1995). X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell 82: 507-522.
27. Haeseleer, F., Sokal, I., Li, N., Pettenati, M., Rao, N., Bronson, D., Wechter, R., Baehr, W., and Palczewski, K. (1999). Molecular characterization of a third member of the guanylyl cyclaseactivating protein subfamily. J. Biol. Chem. 274: 6526-6535.
28. Haire, S.E., Pang, J., Boye, S.L., Sokal, I., Craft, C.M., Palczewski, K., Hauswirth, W.W., and Semple-Rowland, S.L. (2006). Light-Driven Cone Arrestin Translocation in Cones of Postnatal Guanylate Cyclase-1 Knockout Mouse Retina Treated with AAV-GC1. Invest Ophthalmol. Vis. Sci 47: 3745-3753.
29. Hallett, M.A., Delaat, J.L., Arikawa, K., Schlamp, C.L., Kong, F., and Williams, D.R. (1996). Distribution of guanylate cyclase within photoreceptor outer segments. J. Cell Sci. 109: 1803-1812.
30. Hanein, S., Perrault, I., Gerber, S., Tanguy, G., Barbet, F., Ducroq, D., Calvas, P., Dollfus, H., Hamel, C., Lopponen, T., Munier, F., Santos, L., Shalev, S., Zafeiriou, D., Dufier, J.L., Munnich, A., Rozet, J.M., and Kaplan, J. (2004). Leber congenital amaurosis: comprehensive survey of the genetic heterogeneity, refinement of the clinical definition, and genotype-phenotype correlations as a strategy for molecular diagnosis. Hum. Mutat. 23: 306-317.
31. Howes, K.A., Bronson, J.D., Dang, Y.L., Li, N., Zhang, K., Ruiz, C.C., Helekar, B.S., Lee, M., Subbaraya, I., Kolb, H., Chen, J., and Baehr, W. (1998). Gene array and expression of mouse retina guanylate cyclase activating proteins 1 and 2. Invest. Ophthalmol. & Vis. Sci. 39: 867-875.
32. Howes, K.A., Pennesi, M.E., Sokal, I., Church-Kopish, J., Schmidt, B., Margolis, D., Frederick, J.M., Rieke, F., Palczewski, K., Wu, S.M., Detwiler, P.B., and Baehr, W. (2002). GCAP1 rescues rod photoreceptor response in GCAP1/GCAP2 knockout mice. EMBO J. 21: 1545-1554.
33. Hurley, J.B. and Dizhoor, A.M. (2000). Heterologous expression and assays for photoreceptor guanylyl cyclases and guanylyl cyclase activating proteins. Methods Enzymol. 315: 708-717.
34. Imanishi, Y., Li, N., Sowa, M.E., Lichtarge, O., Wensel, T.G., Saperstein, D.A., Baehr, W., and Palczewski, K. (2002). Characterization of retinal guanylate cyclase-activating protein 3 (GCAP3) from zebrafish to man. Eur. J. Neurosci. 15: 63-78.
35. Imanishi, Y., Yang, L., Sokal, I., Filipek, S., Palczewski, K., and Baehr, W. (2004). Diversity of guanylate cyclase-activating proteins (GCAPs) in teleost fish: Characterization of three novel GCAPs (GCAP4, GCAP5, GCAP7) from zebrafish (Danio rerio) and prediction of eight GCAPs (GCAP1-8) in pufferfish (Fugu rubripes). J. Mol. Evol. 59: 204-217.
36. Ito, S., Nakamura, M., Nuno, Y., Ohnishi, Y., Nishida, T., and Miyake, Y. (2004a). Novel complex GUCY2D mutation in Japanese family with cone-rod dystrophy. Invest Ophthalmol. Vis. Sci 45: 1480-1485.
37. Ito, S., Nakamura, M., Ohnishi, Y., and Miyake, Y. (2004b). Autosomal dominant cone-rod dystrophy with R838H and R838C mutations in the GUCY2D gene in Japanese patients. Jpn. J. Ophthalmol. 48: 228-235.
38. Jiang, L., Katz, B.J., Yang, Z., Zhao, Y., Faulkner, N., Hu, J., Baird, J., Baehr, W., Creel, D.J., and Zhang, K. (2005). Autosomal dominant cone dystrophy caused by a novel mutation in the GCAP1 gene (GUCA1A). Mol. Vis. 11: 143-151.
39. Kelsell, R.E., Gregory-Evans K, Payne, A.M., Perrault, I., Kaplan, J., Yang, R.-B., Garbers, D.L., Bird, A.C., Moore, A.T., and Hunt, D.F. (1998). Mutations in the retinal guanylate cyclase (RETGC-1) gene in dominant con-rod dystrophy. Hum. Mol. Genet. 7: 1179-1184.
40. Koch, K.W., Duda, T., and Sharma, R.K. (2002). Photoreceptor specific guanylate cyclases in vertebrate phototransduction. Mol. Cell Biochem. 230: 97-106.
41. Krispel, C.M., Chen, D., Melling, N., Chen, Y.J., Martemyanov, K.A., Quillinan, N., Arshavsky, V.Y., Wensel, T.G., Chen, C.K., and Burns, M.E. (2006). RGS Expression Rate-Limits Recovery of Rod Photoresponses. Neuron 51: 409-416.
42. Krylov, D.M. and Hurley, J.B. (2001). Identification of proximate regions in a complex of retinal guanylyl cyclase 1 and guanylyl cyclase activating protein-1 by a novel mass spectrometry based method. J Biol. Chem. 276: 30648-30654.
43. Krylov, D.M., Niemi, G.A., Dizhoor, A.M., and Hurley, J.B. (1999). Mapping Sites in Guanylyl Cyclase Activating Protein-1 Required for Regulation of Photoreceptor Membrane Guanylyl Cyclases. J. Biol. Chem. 274: 10833-10839.
44. Laura, R.P., Dizhoor, A.M., and Hurley, J.B. (1996). The membrane guanylyl cyclase, retinal guanylyl cyclase-1, is activated through its intracellular domain. J. Biol. Chem. 271: 11646-11651.
45. Laura, R.P. and Hurley, J.B. (1998). The kinase homology domain of retinal guanylyl cyclases 1 and 2 specifies the affinity and cooperativity of interaction with guanylyl cyclase activating protein-2. Biochemistry 37: 11264-11271.
46. LaVail, M.M., Yasumura, D., Matthes, M.T., Drenser, K.A., Flannery, J.G., Lewin, A.S., and Hauswirth, W.W. (2000). Ribozyme rescue of photoreceptor cells in P23H transgenic rats: long- term survival and late-stage therapy. Proc. Natl. Acad. Sci. U. S. A 97: 11488-11493.
47. Lewit-Bentley, A. and Rety, S. (2000). EF-hand calcium-binding proteins. Curr. Opin. Struct. Biol. 10: 637-643.
48. Liu, X., Seno, K., Nishizawa, Y., Hayashi, F., Yamazaki, A., Matsumoto, H., Wakabayashi, T., and Usukura, J. (1994). Ultrastructural localization of retinal guanylate cyclase in human and monkey retinas. Exp. Eye Res. 59: 761-768.
49. Lowe, D.G., Dizhoor, A.M., Liu, K., Gu, Q., Spencer, M., Laura, R., Lu, L., and Hurley, J.B. (1995). Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2. Proc. Natl. Acad. Sci. USA 92: 5535-5539.
50. Lyubarsky, A.L., Naarendorp, F., Zhang, X., Wensel, T., Simon, M.I., and Pugh, E.N., Jr. (2001). RGS9-1 is required for normal inactivation of mouse cone phototransduction. Mol. Vis. 7: 71-78.
51. McBee, J.K., Palczewski, K., Baehr, W., and Pepperberg, D.R. (2001). Confronting complexity: the interlink of phototransduction and retinoid metabolism in the vertebrate retina. Prog. Retin. Eye Res. 20: 469-529.
52. Mendez, A., Burns, M.E., Sokal, I., Dizhoor, A.M., Baehr, W., Palczewski, K., Baylor, D.A., and Chen, J. (2001). Role of guanylate cyclase-activating proteins (GCAPs) in setting the flash sensitivity of rod photoreceptors. Proc. Natl. Acad. Sci. U. S. A 98: 9948-9953.
53. Michaelides, M., Wilkie, S.E., Jenkins, S., Holder, G.E., Hunt, D.M., Moore, A.T., and Webster, A.R. (2005). Mutation in the gene GUCA1A, encoding guanylate cyclase-activating protein 1, causes cone, cone-rod, and macular dystrophy. Ophthalmology 112: 1442-1447.
54. Nakayama, S., Moncrief, N.D., and Kretsinger, R.H. (1992). Evolution of EF-hand calcium-modulated proteins II. Domains of several subfamilies have diverse evolutionary histories. J. Mol. Evol. 34: 416-448.
55. Newbold, R.J., Deery, E.C., Payne, A.M., Wilkie, S.E., Hunt, D.M., and Warren, M.J. (2002). Guanylate cyclase activating proteins, guanylate cyclase and disease. Adv. Exp. Med. Biol. 514: 411-438.
56. Newbold, R.J., Deery, E.C., Walker, C.E., Wilkie, S.E., Srinivasan, N., Hunt, D.M., Bhattacharya, S.S., and Warren, M.J. (2001). The destabilization of human GCAP1 by a proline to leucine mutation might cause cone-rod dystrophy. Hum. Mol. Genet 10: 47-54.
57. Nishiguchi, K.M., Sokal, I., Yang, L., Roychowdhury, N., Palczewski, K., Berson, E.L., Dryja, T.P., and Baehr, W. (2004). A Novel Mutation (I143NT) in Guanylate Cyclase-Activating Protein 1 (GCAP1) Associated with Autosomal Dominant Cone Degeneration. Invest Ophthalmol. Vis. Sci 45: 3863-3870.
58. Olshevskaya, E.V., Boikov, S., Ermilov, A., Krylov, D., Hurley, J.B., and Dizhoor, A.M. (1999a). Mapping Functional Domains of the Guanylate Cyclase Regulator Protein, GCAP-2. J. Biol. Chem. 274: 10823-10832.
59. 2+ and causes photoreceptor degeneration in transgenic mice. J. Neurosci. 24: 6078-6085.
60. Olshevskaya, E.V., Ermilov, A.N., and Dizhoor, A.M. (1999b). Dimerization of guanylyl cyclaseactivating protein and a mechanism of photoreceptor guanylyl cyclase activation. J. Biol. Chem. 274: 25583-25587.
61. Otto-Bruc, A., Buczylko, J., Surgucheva, I., Subbaraya, I., Rudnicka-Nawrot, M., Crabb, J., Arendt, A., Hargrave, P.A., Baehr, W., and Palczewski, K. (1997a). Functional reconstitution of photoreceptor guanylate cyclase with native and mutant forms of guanylate cyclase activating protein 1. Biochemistry 36: 4295-4302.
62. Otto-Bruc, A., Fariss, R.N., Haeseleer, F., Huang, J., Buczylko, J., Surgucheva, I., Baehr, W., Milam, A.H., and Palczewski, K. (1997b). Localization of guanylate cyclase activating protein 2 in mammalian retinas. Proc. Natl. Acad. Sci. U. S. A 94: 4727-4732.
63. Padmanabhan, B., Kuzuhara, T., Adachi, N., and Horikoshi, M. (2004). The crystal structure of CCG1/TAF(II)250-interacting factor B (CIB). J. Biol. Chem. 279: 9615-9624.
64. Palczewski, K., Polans, A.S., Baehr, W., and Ames, J.B. (2000). Calcium binding proteins in the retina: Structure, function, and the etiology of human visual diseases. BioEssays 22: 337-350.
65. Palczewski, K., Sokal, I., and Baehr, W. (2004). Guanylate cyclase-activating proteins: structure, function, and diversity. Biochem. Biophys. Res. Commun. 322: 1123-1130.
66. Payne, A.M., Downes, S.M., Bessant, D.A., Taylor, R., Holder, G.E., Warren, M.J., Bird, A.C., and Bhattacharya, S.S. (1998). A mutation in guanylate cyclase activator 1A (GUCA1A) in an autosomal dominant cone dystrophy pedigree mapping to a new locus on chromosome 6p21.1. Hum. Mol. Genet. 7: 273-277.
67. Payne, A.M., Morris, A.G., Downes, S.M., Johnson, S., Bird, A.C., Moore, A.T., Bhattacharya, S.S., and Hunt, D.M. (2001). Clustering and frequency of mutations in the retinal guanylate cyclase (GUCY2D) gene in patients with dominant cone-rod dystrophies. J. Med. Genet. 38: 611-614.
68. Pennesi, M.E., Howes, K.A., Baehr, W., and Wu, S.M. (2003). Guanylate cyclase-activating protein (GCAP) 1 rescues cone recovery kinetics in GCAP1/GCAP2 knockout mice. Proc. Natl. Acad. Sci U. S. A 100: 6783-6788.
69. Perrault, I., Hanein, S., Gerber, S., Lebail, B., Vlajnik, P., Barbet, F., Ducroq, D., Dufier, J.L., Munnich, A., Kaplan, J., and Rozet, J.M. (2005). A novel mutation in the GUCY2D gene responsible for an early onset severe RP different from the usual GUCY2D-LCA phenotype. Hum. Mutat. 25: 222.
70. Perrault, I., Rozet, J.M., Gerber, S., Ghazi, I., Ducroq, D., Souied, E., Leowski, C., Bonnemaison, M., Dufier, J.L., Munnich, A., and Kaplan, J. (2000). Spectrum of retGC1 mutations in Leber's congenital amaurosis. Eur. J. Hum. Genet. 8: 578-582.
71. Perrault, I., Rozet, J.M., Gerber, S., Kelsell, R.E., Souied, E., Cabot, A., Hunt, D.M., Munnich, A., and Kaplan, J. (1998). A retGC-1 mutation in autosomal dominant cone-rod dystrophy. Am. J. Hum. Genet. 63: 651-654.
72. Perrault, I., Rozet, J.-M., Calvas, P., Gerber, S., Camuzat, A., Dollfus, H., Chatelin, S., Souied, E., Ghazi, I., Leowski, C., Bonnermaison, M., Le Paslier, D., Frezal, J., Dufier, J.-L., Pittler, S.J., Munnich, A., and Kaplan, J. (1996). Retinal-specific guanylate cyclase gene mutations in Leber's congenital amaurosis. Nature Genet. 14: 461-464.
73. 2+ binding proteins in the retina. Trends Neurosci. 19: 547-554.
74. Pugh, E.N., Jr., Duda, T., Sitaramayya, A., and Sharma, R.K. (1997). Photoreceptor guanylate cyclases: a review. Biosci. Rep. 17: 429-473.
75. Pugh, E.N., Jr., Nikonov, S., and Lamb, T.D. (1999). Molecular mechanisms of vertebrate photoreceptor light adaptation. Curr. Opin. Neurobiol. 9: 410-418.
76. Rozet, J.M., Perrault, I., Gerber, S., Hanein, S., Barbet, F., Ducroq, D., Souied, E., Munnich, A., and Kaplan, J. (2001). Complete abolition of the retinal-specific guanylyl cyclase (retGC-1) catalytic ability consistently leads to leber congenital amaurosis (LCA). Invest Ophthalmol. Vis. Sci 42: 1190-1192.
77. Rudnicka-Nawrot, M., Surgucheva, I., Hulmes, J.D., Haeseleer, F., Sokal, I., Crabb, J.W., Baehr, W., and Palczewski, K. (1998). Changes in biological activity and folding of guanylate cyclase-activating protein 1 as a function of calcium. Biochemistry 37: 248-257.
78. Sato, M., Nakazawa, M., Usui, T., Tanimoto, N., Abe, H., and Ohguro, H. (2005). Mutations in the gene coding for guanylate cyclase-activating protein 2 (GUCA1B gene) in patients with autosomal dominant retinal dystrophies. Graefes Arch. Clin. Exp. Ophthalmol. 243: 235-242.
79. Seebacher, T., Beitz, E., Kumagami, H., Wild, K., Ruppersberg, J.P., and Schultz, J.E. (1999). Expression of membrane-bound and cytosolic guanylyl cyclases in the rat inner ear. Hear. Res. 127: 95-102.
80. Semple-Rowland, S.L., Lee, N.R., Van Hooser, J.P., Palczewski, K., and Baehr, W. (1998). A null mutation in the photoreceptor guanylate cyclase gene causes the retinal degeneration chicken phenotype. Proc. Natl. Acad. Sci. USA 95: 1271-1276.
81. Sitaramayya, A., Duda, T., and Sharma, R.K. (1995). Regulation of bovine rod outer segment membrane guanylate cyclase by ATP. Mol. Cell. Biochem. 148: 139-145.
82. Sokal, I., Alekseev, A., Baehr, W., Haeseleer, F., and Palczewski, K. (2002). Soluble fusion proteins between single transmembrane photoreceptor guanylyl cyclases and their activators. Biochemistry 41: 251-257.
83. Sokal, I., Dupps, W.J., Andorf, J.A., Schrum, K.M., Melendez, K.A., Roychowdhury, N., Yang, L., Filipek, S., Palczewski, K., Stone, E.M., and Baehr, W. (2004). A Novel GCAP1 Missense Mutation (L151F) in a Large Family with Autosomal Dominant Cone-Rod Dystrophy. Invest Ophthalmol. Vis. Sci submitted.
84. 2+-binding proteins in the retina: from discovery to etiology of human disease. Biochim. Biophys. Acta 1498: 233-251.
85. Sokal, I., Otto-Bruc, A.E., Surgucheva, I., Verlinde, C.L., Wang, C.K., Baehr, W., and Palczewski, K. (1999). Conformational changes in guanylyl cyclase-activating protein 1 (GCAP1) and its tryptophan mutants as a function of calcium concentration. J. Biol. Chem. 274: 19829-19837.
86. Stephen, R., Palczewski, K., and Sousa, M.C. (2006). The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies. J. Mol. Biol. 359: 266-275.
87. Tucker, C.L., Ramamurthy, V., Pina, A.L., Loyer, M., Dharmaraj, S., Li, Y., Maumenee, I.H., Hurley, J.B., and Koenekoop, R.K. (2004). Functional analyses of mutant recessive GUCY2D alleles identified in Leber congenital amaurosis patients: protein domain comparisons and dominant negative effects. Mol. Vis. 10: 297-303.
88. Tucker, C.L., Woodcock, S.C., Kelsell, R.E., Ramamurthy, V., Hunt, D.M., and Hurley, J.B. (1999). Biochemical analysis of a dimerization domain mutation in RetGC-1 associated with dominant conerod dystrophy. Proc. Natl. Acad. Sci. U. S. A 96: 9039-9044.
89. Van Ghelue, M., Eriksen, H.L., Ponjavic, V., Fagerheim, T., Andreasson, S., Forsman-Semb, K., Sandgren, O., Holmgren, G., and Tranebjaerg, L. (2000). Autosomal dominant cone-rod dystrophy due to a missense mutation (R838C) in the guanylate cyclase 2D gene (GUCY2D) with preserved rod function in one branch of the family. Ophthalmic Genet 21: 197-209.
90. Vijay-Kumar, S. and Kumar, V.D. (1999). Crystal structure of recombinant bovine neurocalcin. Nat. Struct. Biol. 6: 80-88.
91. Wilkie, S.E., Li, Y., Deery, E.C., Newbold, R.J., Garibaldi, D., Bateman, J.B., Zhang, H., Lin, W., Zack, D.J., Bhattacharya, S.S., Warren, M.J., Hunt, D.M., and Zhang, K. (2001). Identification and functional consequences of a new mutation (E155G) in the gene for GCAP1 that causes autosomal dominant cone dystrophy. Am. J Hum. Genet 69: 471-480.
92. Williams, M.L., Coleman, J.E., Haire, S.E., Aleman, T.S., Cideciyan, A.V., Sokal, I., Palczewski, K., Jacobson, S.G., and Semple-Rowland, S.L. (2006). Lentiviral expression of retinal guanylate cyclase-1 (RetGC1) restores vision in an avian model of childhood blindness. PLoS. Med. 3: e201.
93. Yamazaki, A., Yamazaki, M., Yamazaki, R.K., and Usukura, J. (2006). Illuminated rhodopsin is required for strong activation of retinal guanylate cyclase by guanylate cyclase-activating proteins. Biochemistry 45: 1899-1909.
94. Yamazaki, M., Usukura, J., Yamazaki, R.K., and Yamazaki, A. (2005). ATP binding is required for physiological activation of retinal guanylate cyclase. Biochem. Biophys. Res. Commun. 338: 1291-1298.
95. Yang, R.B., Fulle, H.J., and Garbers, D.L. (1996). Chromosomal localization and genomic organization of genes encoding guanylyl cyclase receptors expressed in olfactory sensory neurons and retina. Genomics 31: 367-372.
96. Yang, R.B. and Garbers, D.L. (1997). Two eye guanylyl cyclases are expressed in the same photoreceptor cells and form homomers in preference to heteromers. J. Biol. Chem. 272: 13738-13742.
97. Yang, R.B., Robinson, S.W., Xiong, W.H., Yau, K.W., Birch, D.G., and Garbers, D.L. (1999). Disruption of a retinal guanylyl cyclase gene leads to cone-specific dystrophy and paradoxical rod behavior. J. Neurosci. 19: 5889-5897.
98. 2+-binding proteins involves its dimerization. J. Biol. Chem. 274: 15547-15555.