Altered functionality in rhodopsin point mutants associated with retinitis pigmentosa

Biochemical and Biophysical Research Communications

Volumn 303, Issue 1, 2003, Pages 294-301

  Andrés, Anna ^a   Garriga, Pere ^b   Manyosa, Joan ^a  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b UNIVERSITAT POLITÈCNICA DE CATALUNYA   (Spain)

Author keywords

G protein coupled receptor; Protein misfolding; Retinitis pigmentosa; Transducin activation

Indexed keywords

11 CIS RETINAL; RHODOPSIN; HYDROXYLAMINE; OPSIN; TRANSDUCIN;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL STRAIN COS1; CONTROLLED STUDY; CYTOPLASM; MUTATION; NONHUMAN; PHOTOTRANSDUCTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RETINA DEGENERATION; RETINITIS PIGMENTOSA; STOICHIOMETRY; AMINO ACID SEQUENCE; ANIMAL; ENZYME ACTIVATION; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; POINT MUTATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPECTROPHOTOMETRY; ULTRAVIOLET RADIATION; WESTERN BLOTTING;

MAMMALIA;

AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; COS CELLS; CYTOPLASM; ENZYME ACTIVATION; HUMANS; HYDROXYLAMINES; MOLECULAR SEQUENCE DATA; MUTATION; OPSIN; POINT MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RETINITIS PIGMENTOSA; RHODOPSIN; SPECTROPHOTOMETRY; TRANSDUCIN; ULTRAVIOLET RAYS;

EID: 0037470723     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00328-0     Document Type: Article

References (50)

1. Farrar G.J., Kennan P.F., Humphries P. On the genetics of Retinitis Pigmentosa and on mutation-independent approaches to therapeutic intervention. EMBO J. 21:2002;857-864.
2. Wang Q., Chen Q., Zhao K., Wang L., Wang L., Traboulsi E.I. Update on the molecular genetics of retinitis pigmentosa. Ophthal. Genet. 22:2001;133-154.
3. Berson E.L. Retinitis pigmentosa. The Friendenwald lecture. Invest. Ophthalmol. Vis. Sci. 34:1993;1659-1676.
4. Heckenlively J.R. Retinitis Pigmentosa. 1988;J.B. Lippincott, Philadelphia.
5. Phelan J.K., Bok D. A brief review of RP and the identified RP genes. Mol. Vis. 6:2000;116-124.
6. Hargrave P.A. Rhodopsin structure, function, and topology. The Friedenwald lecture. Invest. Ophthalmol. Vis. Sci. 42:2001;3-9.
7. Pepe I.M. Recent advances of our understanding of rhodopsin and phototransduction. Prog. Retin. Eye Res. 20:2001;733-759.
8. Sakmar T.P., Menon S.T., Marin E.P., Awad E.S. Rhodopsin insights from recent structural studies. Annu. Rev. Biophys. Biomol. Struct. 31:2002;443-484.
9. Donnely D., Findlay J.B.C. Seven-helix receptors: structure and modelling. Curr. Opin. Struct. Biol. 4:1994;582-589.
10. Wess J. G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J. 11:1997;346-354.
11. Ji T.H., Grossmann M., Ji I. G protein-coupled receptors. I. Diversity of receptor-ligand interactions. J. Biol. Chem. 273:1998;17299-17302.
12. Bockaert J., Pin J.P. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 18:1999;1723-1729.
13. Palczewski K., Kumasaka T., Hori T., Behnke C.A., Motoshima H., Fox B.A., Le Trong I., Teller D.C., Okada T., Stenkamp R.E., Yamamoto M., Miyano M. Crystal structure of rhodopsin: a G protein-coupled receptor. Science. 289:2000;739-745.
14. Teller D.C., Okada T., Behnke C.A., Palczewski K., Stenkamp R.E. Advances in determintation of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry. 40:2001;7761-7772.
15. Okada T., Fujiyoshi Y., Silow M., Navarro J., Landau E.M., Shichida Y. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc. Natl. Acad. Sci. USA. 99:2002;5982-5987.
16. Robinson P.R., Cohen G.B., Zhukovsky E.A., Oprian D.D. Constitutively active mutants of rhodopsin. Neuron. 367:1992;639-642.
17. Rao V.K., Oprian D.D. Activation mutations of rhodopsin and other G protein-coupled receptors. Annu. Rev. Biophys. Biomol. Struct. 25:1996;287-314.
18. Sheikh S.P., Zvyaga T.A., Lichtarge A., Sakmar T.P., Bourne H.R. Rhodopsin activation blocked by metal-ion-binding sites linking trasmembrane helices C and F. Nature. 383:1996;347-350.
19. Farrens D.L., Altenbach C., Yang K., Hubbell W.L., Khorana H.G. Requirement of rigid-body motion of trasmembrane helices for light activation of rhodopsin. Science. 274:1996;768-770.
20. Okada T., Ernst O.P., Palczewski K., Hofmann K.P. Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem. Sci. 26:2001;318-324.
21. Arnis S., Hofmann K.P. Photoregeneration of bovine rhodopsin from its signalling state. Biochemistry. 34:1995;9333-9340.
22. Franke R.R., Konig B., Sakmar T.P., Khorana H.G., Hofmann K.P. Rhodopsin mutants that bind but fail to activate transducin. Science. 250:1990;123-125.
23. Acharya S., Karnik S.S. Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin. J. Biol. Chem. 271:1996;25406-25411.
24. Min K.C., Zvyaga T.A., Cypess A.M., Sakmar T.P. Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. J. Biol. Chem. 268:1993;9400-9404.
25. Sung C.H., Davenport C.M., Nathans J. Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. J. Biol. Chem. 268:1993;26645-26649.
26. Kaushal S., Khorana H.G. Structure and function in rhodopsin 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry. 33:1994;6121-6128.
27. Ridge K.D., Lu Z., Liu X., Khorana H.G. Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons. Biochemistry. 34:1995;3261-3267.
28. Liu X., Garriga P., Khorana H.G. Structure and function in rhodopsin: correct folding and misfolding in two point mutants in the intradiscal domain of rhodopsin identified in retinitis pigmentosa. Proc. Natl. Acad. Sci. USA. 93:1996;4554-4559.
29. Garriga P., Liu X., Khorana H.G. Structure and function in rhodopsin: correct folding and misfolding in point mutants at and in proximity to the site of the retinitis pigmentosa mutation Leu-125. → Arg in the transmembrane helix C Proc. Natl. Acad. Sci. USA. 93:1996;4560-4564.
30. Ferretti L., Karnik S.S., Khorana H.G., Nassal M., Oprian D.D. Total synthesis of a gene for bovine rhodopsin. Proc. Natl. Acad. Sci. USA. 83:1986;599-603.
31. Franke R.R., Sakmar T.P., Oprian D.D., Khorana H.G. A single amino acid substitution in rhodopsin (lysine248-leucine) prevents activation of transducin. J. Biol. Chem. 263:1988;2119-2122.
32. Oprian D.D., Molday R.S., Kaufman R.J., Khorana H.G. Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proc. Natl. Acad. Sci. USA. 84:1987;8874-8878.
33. Andrés A., Kosoy A., Garriga P., Manyosa J. Mutations at position 125 in transmembrane helix III of rhodopsin affect the structure and signalling of the receptor. Eur. J. Biochem. 268:2001;5696-5704.
34. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
35. Burnette W.N. "Western Blotting:" electrophoretic transfer of proteins from sodium dodecylsulfate polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:1981;195-203.
36. Ting T.D., Goldin S.B., Ho Y.K. Purification and characterization of bovine transducin and its subunits. Hargrave P.A. Methods in Neurosciences. 15:1994;180-195 Academic Press, San Diego, CA.
37. Han M., Lin S.W., Smith S.O., Sakmar T.P. The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin. J. Biol. Chem. 271:1996;32330-32336.
38. Kaushal S., Ridge K.D., Khorana H.G. Structure and function in rhodopsin: the role of asparagines-linked glycosylation. Proc. Natl. Acad. Sci. USA. 91:1994;4024-4028.
39. Ballesteros J.A., Jensen A.D., Liapakis G., Rasmussen S.G., Shi L., Gether U., Javitch J.A. Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 276:2001;29171-29177.
40. Sung C.H., Tai A.W. Rhodopsin trafficking and its role in retinal dystrophies. Int. Rev. Cytol. 195:2000;215-267.
41. Concepcion F., Mendez A., Chen J. The carboxy-terminal domain is essential for rhodopsin transport in rod photoreceptors. Vision Res. 42:2002;417-426.
42. Berson E.L., Rosner B., Weigel-DiFranco C., Dryja T., Sandberg M.A. Disease progression in patients with dominant retinitis pigmentosa and rhodopsin mutations. Invest. Ophthalmol. Vis. Sci. 43:2002;3027-3036.
43. al-Jandal N., Farrar G.J., Kiang A.S., Humphries M.M., Bannon N., Findlay J.B., Humphries P., Kenna P.F. A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal dominant congenital stationary night blindness. Hum. Mutat. 13:1991;75-81.
44. Ramon E., Valle L.J., Garriga P. Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr94Ile. J. Biol. Chem. 278:2003;6427-6432.
45. Gross A.K., Rao V.K., Oprian D.D. Characterization of rhodopsin congenital night blindness mutant T94I. Biochemistry. 42:2003;2009-2015.
46. Garriga P., Manyosa J. The eye photoreceptor protein rhodopsin. Structural implications for retinal disease. FEBS Lett. 528:2002;17-22.
47. Hamm H.E. How activated receptors couple to G proteins. Proc. Natl. Acad. Sci. USA. 98:2001;4819-4821.
48. 2+ and photoreceptor death: new evidence for the equivalent-light hypothesis from arrestin knowckout mice Invest. Ophthalmol. Vis. Sci. 40:1999;2770-2772.
49. Lisman J., Fain G. Support for equivalent light hypothesis for RP. Nat. Med. 1:1995;1254-1255.
50. Travis G.H. Mechanisms of cell death in the inherited retinal degenerations. Am. J. Hum. Genet. 62:1998;503-508.