Receptor and βγ binding sites in the α subunit of the retinal G protein transducin

Science

Volumn 275, Issue 5298, 1997, Pages 381-384

  Onrust, René ^a,b   Herzmark, Paul ^a   Chi, Patty ^a   Garcia, Pablo D ^a   Lichtarge, Olivier ^a   Kingsley, Chris ^a   Bourne, Henry R ^c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Genesis Research & Development Corporation Ltd   (New Zealand)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE RECEPTOR; ALUMINUM DERIVATIVE; ALUMINUM FLUORIDE; FLUORIDE; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; RETINAL; RHODOPSIN; TRANSDUCIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; NEUROTRANSMISSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; RECEPTOR BINDING; RETINA; SIGNAL TRANSDUCTION; ANIMAL; CELL STRAIN COS1; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MUTATION; PHENOTYPE; PROTEIN CONFORMATION; RETINA ROD OUTER SEGMENT;

ALUMINUM COMPOUNDS; ANIMALS; BINDING SITES; COS CELLS; FLUORIDES; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE); GUANOSINE DIPHOSPHATE; MODELS, MOLECULAR; MUTATION; PHENOTYPE; PROTEIN CONFORMATION; RETINALDEHYDE; RHODOPSIN; ROD OUTER SEGMENTS; TRANSDUCIN;

EID: 0030614427     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5298.381     Document Type: Article

References (43)

1. H. R. Bourne, D. A. Sanders, F. McCormick, Nature 348, 125 (1990); L. Birnbaumer, Annu. Rev. Pharmacol. Toxicol. 30, 675 (1990); A. H. Cheung, R. R. Huang, C. D. Strader, Mol. Pharmacol. 41, 1061 (1992); M. Freissmuth, P. J. Casey, A. G. Gilman, FASEB J. 3, 2125 (1989); Y. Kaziro, H. Itoh, T. Kozasa, M. Nakafuku, T. Satoh, Annu. Rev. Biochem. 60, 349 (1991); E. J. Neer, Cell 80, 249 (1995).
2. H. R. Bourne, D. A. Sanders, F. McCormick, Nature 348, 125 (1990); L. Birnbaumer, Annu. Rev. Pharmacol. Toxicol. 30, 675 (1990); A. H. Cheung, R. R. Huang, C. D. Strader, Mol. Pharmacol. 41, 1061 (1992); M. Freissmuth, P. J. Casey, A. G. Gilman, FASEB J. 3, 2125 (1989); Y. Kaziro, H. Itoh, T. Kozasa, M. Nakafuku, T. Satoh, Annu. Rev. Biochem. 60, 349 (1991); E. J. Neer, Cell 80, 249 (1995).
3. H. R. Bourne, D. A. Sanders, F. McCormick, Nature 348, 125 (1990); L. Birnbaumer, Annu. Rev. Pharmacol. Toxicol. 30, 675 (1990); A. H. Cheung, R. R. Huang, C. D. Strader, Mol. Pharmacol. 41, 1061 (1992); M. Freissmuth, P. J. Casey, A. G. Gilman, FASEB J. 3, 2125 (1989); Y. Kaziro, H. Itoh, T. Kozasa, M. Nakafuku, T. Satoh, Annu. Rev. Biochem. 60, 349 (1991); E. J. Neer, Cell 80, 249 (1995).
4. H. R. Bourne, D. A. Sanders, F. McCormick, Nature 348, 125 (1990); L. Birnbaumer, Annu. Rev. Pharmacol. Toxicol. 30, 675 (1990); A. H. Cheung, R. R. Huang, C. D. Strader, Mol. Pharmacol. 41, 1061 (1992); M. Freissmuth, P. J. Casey, A. G. Gilman, FASEB J. 3, 2125 (1989); Y. Kaziro, H. Itoh, T. Kozasa, M. Nakafuku, T. Satoh, Annu. Rev. Biochem. 60, 349 (1991); E. J. Neer, Cell 80, 249 (1995).
5. H. R. Bourne, D. A. Sanders, F. McCormick, Nature 348, 125 (1990); L. Birnbaumer, Annu. Rev. Pharmacol. Toxicol. 30, 675 (1990); A. H. Cheung, R. R. Huang, C. D. Strader, Mol. Pharmacol. 41, 1061 (1992); M. Freissmuth, P. J. Casey, A. G. Gilman, FASEB J. 3, 2125 (1989); Y. Kaziro, H. Itoh, T. Kozasa, M. Nakafuku, T. Satoh, Annu. Rev. Biochem. 60, 349 (1991); E. J. Neer, Cell 80, 249 (1995).
6. H. R. Bourne, D. A. Sanders, F. McCormick, Nature 348, 125 (1990); L. Birnbaumer, Annu. Rev. Pharmacol. Toxicol. 30, 675 (1990); A. H. Cheung, R. R. Huang, C. D. Strader, Mol. Pharmacol. 41, 1061 (1992); M. Freissmuth, P. J. Casey, A. G. Gilman, FASEB J. 3, 2125 (1989); Y. Kaziro, H. Itoh, T. Kozasa, M. Nakafuku, T. Satoh, Annu. Rev. Biochem. 60, 349 (1991); E. J. Neer, Cell 80, 249 (1995).
7. T. M. Vuong, M. Chabre, L. Stryer, Nature 311, 659 (1984); L. Ramdas, R. M. Disher, T. G. Wensel, Biochemistry 30, 11637 (1991).
8. T. M. Vuong, M. Chabre, L. Stryer, Nature 311, 659 (1984); L. Ramdas, R. M. Disher, T. G. Wensel, Biochemistry 30, 11637 (1991).
9. J. P. Noel, H. E. Hamm, P. B. Sigler, Nature 366, 654 (1993).
10. D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 369, 621 (1994); J. Sondek, D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 372, 276 (1994); D. E. Coleman et al., Science 265, 1405 (1994); M. A. Wall et al., Cell 183, 1047 (1995).
11. D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 369, 621 (1994); J. Sondek, D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 372, 276 (1994); D. E. Coleman et al., Science 265, 1405 (1994); M. A. Wall et al., Cell 183, 1047 (1995).
12. D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 369, 621 (1994); J. Sondek, D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 372, 276 (1994); D. E. Coleman et al., Science 265, 1405 (1994); M. A. Wall et al., Cell 183, 1047 (1995).
13. D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 369, 621 (1994); J. Sondek, D. G. Lambright, J. P. Noel, H. E. Hamm, P. B. Sigler, ibid. 372, 276 (1994); D. E. Coleman et al., Science 265, 1405 (1994); M. A. Wall et al., Cell 183, 1047 (1995).
14. D. G. Lambright et al., Nature 379, 311 (1996).
15. B. K.-K. Fung and C. R. Nash, J. Biol. Chem. 258, 10503 (1983); W. J. Phillips and R. A. Cerione, ibid. 267, 17032 (1992); W. J. Phillips, S. C. Wong, R. A. Cerione, ibid., p. 17040; D. J. Kelleher and G. L. Johnson, Mol. Pharmacol. 34, 452 (1988); O. Kisselev and N. Gautam, J. Biol. Chem. 268, 24519 (1993); A. B. Fawzi et al., ibid. 266, 12194 (1991).
16. B. K.-K. Fung and C. R. Nash, J. Biol. Chem. 258, 10503 (1983); W. J. Phillips and R. A. Cerione, ibid. 267, 17032 (1992); W. J. Phillips, S. C. Wong, R. A. Cerione, ibid., p. 17040; D. J. Kelleher and G. L. Johnson, Mol. Pharmacol. 34, 452 (1988); O. Kisselev and N. Gautam, J. Biol. Chem. 268, 24519 (1993); A. B. Fawzi et al., ibid. 266, 12194 (1991).
17. B. K.-K. Fung and C. R. Nash, J. Biol. Chem. 258, 10503 (1983); W. J. Phillips and R. A. Cerione, ibid. 267, 17032 (1992); W. J. Phillips, S. C. Wong, R. A. Cerione, ibid., p. 17040; D. J. Kelleher and G. L. Johnson, Mol. Pharmacol. 34, 452 (1988); O. Kisselev and N. Gautam, J. Biol. Chem. 268, 24519 (1993); A. B. Fawzi et al., ibid. 266, 12194 (1991).
18. B. K.-K. Fung and C. R. Nash, J. Biol. Chem. 258, 10503 (1983); W. J. Phillips and R. A. Cerione, ibid. 267, 17032 (1992); W. J. Phillips, S. C. Wong, R. A. Cerione, ibid., p. 17040; D. J. Kelleher and G. L. Johnson, Mol. Pharmacol. 34, 452 (1988); O. Kisselev and N. Gautam, J. Biol. Chem. 268, 24519 (1993); A. B. Fawzi et al., ibid. 266, 12194 (1991).
19. B. K.-K. Fung and C. R. Nash, J. Biol. Chem. 258, 10503 (1983); W. J. Phillips and R. A. Cerione, ibid. 267, 17032 (1992); W. J. Phillips, S. C. Wong, R. A. Cerione, ibid., p. 17040; D. J. Kelleher and G. L. Johnson, Mol. Pharmacol. 34, 452 (1988); O. Kisselev and N. Gautam, J. Biol. Chem. 268, 24519 (1993); A. B. Fawzi et al., ibid. 266, 12194 (1991).
20. B. K.-K. Fung and C. R. Nash, J. Biol. Chem. 258, 10503 (1983); W. J. Phillips and R. A. Cerione, ibid. 267, 17032 (1992); W. J. Phillips, S. C. Wong, R. A. Cerione, ibid., p. 17040; D. J. Kelleher and G. L. Johnson, Mol. Pharmacol. 34, 452 (1988); O. Kisselev and N. Gautam, J. Biol. Chem. 268, 24519 (1993); A. B. Fawzi et al., ibid. 266, 12194 (1991).
21. Reviewed in B. R. Conklin and H. R. Bourne, Cell 73, 631 (1993).
22. K. A. Sullivan et al., Nature 330, 758 (1987); E. A. Dratz et al., ibid. 363, 276 (1993).
23. K. A. Sullivan et al., Nature 330, 758 (1987); E. A. Dratz et al., ibid. 363, 276 (1993).
24. H. E. Hamm et al., Science 241, 832 (1988).
25. P. D. Garcia, R. Onrust, S. M. Bell, T. P. Sakmar, H. R. Bourne, EMBO J. 14, 4460 (1995).
26. t (10).
27. t near either known or postulated rhodopsin-or βγ-interacting residues (3-5).
28. S. Osawa and E. R. Weiss, J. Biol. Chem. 270, 31052 (1995).
29. t that could bind to rhodopsin but would not be susceptible to rhodopsin-catalyzed replacement of GDP by GTP-γ-S. A mutant rhodopsin with this phenotype has been described (O. P. Ernst, K. P. Hofmann, T. P. Sakmar, ibid., p. 10580).
30. J. Bigay, P. Deterre, C. Pfister, M. Chabre, FEBS Lett. 191, 181 (1985); P. C. Sternweis and A. G. Gilman, Proc. Natl. Acad. Sci. U.S.A. 79, 4888 (1982).
31. J. Bigay, P. Deterre, C. Pfister, M. Chabre, FEBS Lett. 191, 181 (1985); P. C. Sternweis and A. G. Gilman, Proc. Natl. Acad. Sci. U.S.A. 79, 4888 (1982).
32. t in COS cells and its translation in vitro affect folding in different ways.
33. Of the 23 residues identified (5) as interacting directly with βγ, we tested 22. By one or the other assay, mutational replacement of 14 of the 22 residues (in 10 mutants) produced an R phenotype, whereas six mutants were WT and two were indeterminable (11).
34. O. Lichtarge, H. R. Bourne, F. E. Cohen, Proc. Natl. Acad. Sci. U.S.A. 93, 7507 (1996). In this theoretical study, residues in cluster 2 and cluster 1 correspond, respectively, to the βγ-and putative 7TMR-interacting surfaces identified in the present work.
35. t. Corresponding β6-α5 loops of other GTPases interact similarly with the guanine ring of bound GDP and GTP [H. R. Bourne, D. A. Sanders, F. McCormick, Nature 349, 117 (1991)].
36. B. M. Denker, C. J. Schmidt, E. J. Neer, J. Biol. Chem. 267, 9998 (1992); B. M. Denker, P. M. Boutin, E. J. Neer, Biochemistry 34, 5544 (1995); L. A. Quilliam et al., Proc. Natl. Acad Sci. U.S.A. 92, 1272 (1995).
37. B. M. Denker, C. J. Schmidt, E. J. Neer, J. Biol. Chem. 267, 9998 (1992); B. M. Denker, P. M. Boutin, E. J. Neer, Biochemistry 34, 5544 (1995); L. A. Quilliam et al., Proc. Natl. Acad Sci. U.S.A. 92, 1272 (1995).
38. B. M. Denker, C. J. Schmidt, E. J. Neer, J. Biol. Chem. 267, 9998 (1992); B. M. Denker, P. M. Boutin, E. J. Neer, Biochemistry 34, 5544 (1995); L. A. Quilliam et al., Proc. Natl. Acad Sci. U.S.A. 92, 1272 (1995).
39. T. C. Thomas, C. J. Schmidt, E. J. Neer, Proc. Natl. Acad. Sci. U.S.A. 90, 10295 (1993).
40. L. A. Feig and G. M. Cooper, Mol. Cell. Biol. 8, 2472 (1988).
41. T. Iiri, P. Herzmark, J. M. Nakamoto, C. Van Dop, H. R. Bourne, Nature 371, 164 (1994).
42. 324 are located very close to the guanine nucleotide-binding pocket (3-5), where they might be expected to alter regulation of GTP-GDP exchange.
43. t immunoblots. R.O. is a Helen Hay Whitney fellow, P.C. was supported by a grant from the Genentech Foundation, P.D.G. was supported in part by funds from Daiichi, and O.L. was supported by funds from the American Heart Association. Supported by NIH grants GM-27800 and CA-54427 (to H.R.B.).