Abstract
Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch—in bacteria, yeast, flies and vertebrates—suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions.
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References
- 1
Jurnak, F. Science 230, 32–36 (1985).
- 2
La Cour, T. F. M., Nyborg, J., Thirup, S. & Clark, B. F. C. EMBO J. 4, 2385–2388 (1985).
- 3
de Vois, A. M. et al. Science 239, 888–893 (1988).
- 4
Pai, E. F. et al. Nature 341, 209–214 (1989).
- 5
Milburn, M. V. et al. Science 247, 939–945 (1990).
- 6
Brünger, A. T. et al. Proc. natn. Acad. Sci. U.S.A. 87, 4849–4853 (1990).
- 7
Kaziro, Y. Biochim. biophys. Acta 505, 95–127 (1978).
- 8
Thompson, R. C. Trends biochem. Sci. 13, 91–93 (1988).
- 9
Neer, E. J. & Clapham, D. E. Nature 333, 129–134 (1988).
- 10
Stryer, L. & Bourne, H. R. Rev. cell. Biol. 2, 391–419 (1986).
- 11
Birnbaumer, L. et al. Kidney Internat. (Suppl.) 32, S14–S37 (1987).
- 12
Freissmuth, M., Caset, P. J. & Gilman, A. G. FASEB J. 3, 2125–2131 (1989).
- 13
Ross, E. M. Neuron 3, 141–152 (1989).
- 14
Romisch, K. et al. Nature 340, 478–482 (1989).
- 15
Bernstein, H. D. et al. Nature 340, 482–486 (1989).
- 16
Hann, B. C., Poritz, M. A. & Walter, P. J. Cell Biol. 109, 3223–3230 (1989).
- 17
Lauffer, L. et al. Nature 318, 334–338 (1985).
- 18
Barbacid, M. A. Rev. Biochem. 56, 779–827 (1987).
- 19
McCormick, F. Cell 56, 5–8 (1989).
- 20
Salminen, A. & Novick, P. J. Cell 49, 527–538 (1987).
- 21
Bacon, R. A., Salminen, A., Ruohola, H., Novick, P. & Ferro-Novick, S. J. Cell Biol. 109, 105–1022 (1989).
- 22
Schmitt, H. D., Wagner, P., Pfaff, E. & Gallwitz, D. Cell 47, 401–412 (1986).
- 23
Segev, N., Mulholland, J. & Botstein, D. Cell 52, 915–924 (1988).
- 24
Bourne, H. R. Cell 53, 669–671 (1988).
- 25
Masters, S. B., Stroud, R. M. & Bourne, H. R. Protein Engng 1, 47–54 (1986).
- 26
Heidman, W. & Bourne, H. R. in G Proteins (eds Birnbaumer, L. & lyengar, R.) 17–40 (Academic, San Diego, 1990).
- 27
Gibbs, J. B. et al. in ADP-ribosylating Toxins and G Proteins. Insights into Signal Transduction (eds Moss, J. & Vaughan, M.) 381–396 (American Society for Microbiology, Washington DC, 1990).
- 28
Price, S. R., Barber, A. & Moss, J. in ADP-ribosylating Toxins and G Proteins. Insights into Signal Transduction (eds Moss, J. & Vaughan, M.) 397–424 (American Society for Microbiology Washington DC, 1990).
- 29
Trahey, M. & McCormick, F. Science 238, 542–545 (1987).
- 30
Gilman, A. G. A. Rev. Biochem. 56, 615–649 (1987).
- 31
Thompson, R. C., Dix, D. B. & Karim, A. M. J. biol. Chem. 261, 4868–4874 (1986).
- 32
Fong, H. K. W., Yoshimoto, K. K., Eversole-Cire, P. & Simon, M. I. Proc. natn. Acad. Sci. U.S.A. 85, 3066–3070 (1988).
- 33
Matsuoka, M., Itoh, H. Kozasa, T. & Kaziro, Y. Proc. natn. Acad. Sci. U.S.A. 85, 5384–5388 (1988).
- 34
Strathmann, M., Wilkie, T. M. & Simon, M. I. Proc. natn. Acad. Sci. U.S.A. 86, 7407–7409 (1989).
- 35
Bourne, H. R. Cold Spring Harbor Symp. quant. Biol. 53, 1019–1031 (1988).
- 36
Bourne, H. R. & DeFranco, A. L. In Oncogenes and the Molecular Origins of Cancer (ed. Weinberg, R.) 97–124 (Cold Spring Harbor Laboratory, New York, 1989).
- 37
Stryer, L. A. Rev. Neurosci. 9, 87–119 (1986).
- 38
Casey, P. J. & Gilman, A. G. J. biol. Chem. 263, 2577–2580 (1988).
- 39
Graziano, M. & Gilman, A. G. J. biol. Chem. 264, 15475–15482 (1989).
- 40
Landis, C. A. et al. Nature 340, 692–696 (1989).
- 41
Dietzel, C. & Kurjan, J. Cell 50, 1001–1010 (1987).
- 42
Nakafuku, M., Itoh, H., Nakamura, S. & Kaziro, Y. Proc. natn. Acad. Sci. U.S.A. 84, 2140–2144 (1987).
- 43
Miyajima, I. et al. Cell 50, 1011–1019 (1987).
- 44
Whiteway, M. et al. Cell 56, 457–477 (1989).
- 45
Bourne, H. R., Coffino, P. & Tomkins, G. M. Science 187, 750–752 (1975).
- 46
Harris, B. A., Robishaw, J. D., Mumby, S. M. & Gilman, A. G. Science 229, 1274–1277 (1985).
- 47
Robinshaw, J. D., Russell, D. W., Harris, B. A., Smigel, M. D. & Gilman, A. G. Proc. natn. Acad. Sci. U.S.A. 83, 1251–1255 (1986).
- 48
Miyajima, I., Arai, K. I. & Matsumoto, K. Molec. cell. Biol. 9, 2289–2297 (1989).
- 49
Bourne, H. R. Nature 337, 504–505 (1989).
- 50
Birchmeier, C., Broek, D. & Wigler, M. Cell 43, 615–621 (1985).
- 51
Bar-Sagi, D. & Feramisco, J. R. Cell 42, 841–848 (1985).
- 52
Satoh, T., Nakamura, S. & Kaziro, Y. Molec. cell. Biol. 7, 4553–4556 (1987).
- 53
John, J., Frech, M. & Wittinghofer, A. J. biol. Chem. 263, 11792–11799 (1988).
- 54
Neal, S. E., Eccleston, J. F., Hall, A. & Webb, M. R. J. biol. Chem. 263, 19718–19722 (1988).
- 55
West, M., Kung, H.-F. & Kamata, T. FEBS Lett. 259, 245–248 (1990).
- 56
Wolfman, A. & Macara, I. G. Science 248, 67–69 (1990).
- 57
Downward, J., Riehl, R., Wu, L. & Weinberg, R. A. Proc. natn. Acad. Sci. U.S.A. 87, 5998–6002 (1990).
- 58
Vogel, U.S. et al. Nature 335, 90–93 (1988).
- 59
Trahey, M. et al. Science 242, 1697–1700 (1988).
- 60
Tabaka, K. et al. Cell 60, 803–807 (1990).
- 61
Sigal, I. S. et al. Proc. natn. Acad. Sci. U.S.A. 83, 952–956 (1986).
- 62
Walter, M., Clark, S. G. & Levinson, A. D. Science 233, 649–652 (1986).
- 63
Feig, L. A. & Cooper, G. M. Molec. cell. Biol. 8, 2472–2478 (1988).
- 64
Ballester, R. et al. Cell 59, 681–686 (1989).
- 65
Zhang, K. et al. Nature 346, 719–723 (1990).
- 66
Downward, J., Graves, J. D., Warne, P. H., Rayter, S. & Cantrell, D. A. Nature 346, 719–723 (1990).
- 67
Gibbs, J. B., Schaber, M. D., Schofield, T. L., Scolnick, E. M. & Sigal, I. S. Proc. natn. Acad. Sci. U.S.A. 86, 6630–6634 (1989).
- 68
Gibbs, J. B. & Marshall, M. S. Microbiol. Rev. 53, 171–185 (1989).
- 69
Hall, A. Cell 61, 921–923 (1990).
- 70
Yatani, A., Okabe, K., Polakis, P., McCormick, F. & Brown, A. M. Cell 61, 769–776 (1990).
- 71
Field, J., Broek, D., Kataoka, T. & Wigler, M. Molec. cell. Biol. 7, 2128–2183 (1987).
- 72
Broek, D. et al. Cell 41, 763–769 (1985).
- 73
Wigler, M. et al. Cold Spring Harbor Symp. quant. Biol. 53, 649–655 (1988).
- 74
Toda, T., Cameron, S., Sass, P., Zoller, M. & Wigler, M. Cell 50, 277–287 (1987).
- 75
Camonis, J. H. et al. EMBO J. 5, 375–380 (1986).
- 76
Broek, D. et al. Cell 48, 789–799 (1987).
- 77
Powers, S., O'Neill, K. & Wigler, M. Molec. cell. Biol. 9, 390–395 (1989).
- 78
Créchet, J.-B. et al. Science 248, 866–868 (1990).
- 79
Ellis, C., Moran, M., McCormick, F. & Pawson, T. Nature 343, 377–381 (1990).
- 80
Molloy, C. J. et al. Nature 342, 711–714 (1989).
- 81
Kaplan, D. R., Morrison, D. K., Wong, G., McCormick, F. & Williams, L. T. Cell 61, 125–133 (1990).
- 82
Kazlauskas, A., Ellis, C., Pawson, T. & Cooper, J. A. Science 247, 1578–1581 (1990).
- 83
Xu, G. et al. Cell 62, 599–608 (1990).
- 84
Garrett, M. D., Self, A. J., van Oers, C. & Hall, A. J. biol. Chem. 264, 10–13 (1989).
- 85
Frech, M. et al. Science 249, 169–171 (1990).
- 86
Hata, Y. et al. J. biol. Chem. 265, 7104–7107 (1990).
- 87
Kikuchi, A., Sasaki, T., Araki, S., Hata, Y. & Takai, Y. J. biol. Chem. 264, 9133–9136 (1989).
- 88
Kitayama, H., Sugimoto, Y., Matsuzaki, T., Ikawa, Y. & Noda, M. Cell 56, 77–84 (1989).
- 89
Sasaki, T. et al. J. biol. Chem. 265, 2333–2337 (1990).
- 90
Ueda, T., Kikuchi, A., Ohga, N., Yamamoto, J. & Takai, Y. J. biol. Chem. 265, 9373–9380 (1990).
- 91
Matsui, Y. et al. Molec. cell. Biol. 10, 4116–4122 (1990).
- 92
Araki, S., Kikuchi, A., Hata, Y., Isomura, M. & Takai, Y. J. biol. Chem. 265, 13007–13015 (1990).
- 93
Gutierrez, L., Magee, A. I., Marshall, C. J. & Hancock, J. F. EMBO J. 8, 1093–1098 (1989).
- 94
Hancock, J. F., Magee, A. I., Childs, J. E. & Marshall, C. J. Cell 57, 1167–1177 (1989).
- 95
Clarke, S., Vogel, J. P., Deschenes, R. J. & Stock, J. Proc. natn. Acad. Sci. U.S.A. 85, 4643–4647 (1988).
- 96
Willumsen, B. M., Christensen, A., Hubbert, N. L., Papageorge, A. G. & Lowy, D. R. Nature 310, 583–586 (1984).
- 97
Walworth, N. C., Goud, B., Kabcenell, A. K. & Novick, P. J. EMBO J. 8, 1685–1693 (1989).
- 98
Molenaar, C. M. T., Prange, R. & Gallwitz, D. EMBO J. 7, 971–976 (1988).
- 99
Maltese, W. A., Sheridan, K. M., Repko, E. M. & Erdman, R. A. J. biol. Chem. 265, 2148–2155 (1990).
- 100
Backlund, P. S. & Aksamit, R. R. J. biol. Chem. 263, 15864–15867 (1988).
- 101
Melancon, P. et al. Cell 51, 1053–1062 (1987).
- 102
Mayorga, L. S., Diaz, R. & Stahl, P. D. Science 244, 1475–1477 (1989).
- 103
Mayorga, L. S., Diaz, R., Colombo, M. I. & Stahl, P. D. Cell Reg. 1, 113–124 (1989).
- 104
Ruohola, H., Kabcenell, A. K. & Ferro-Novick, S. J. Cell Biol. 107, 1465–1476 (1988).
- 105
Baker, D., Hicke, L., Rexach, M., Schleyer, M. & Schekman, R. Cell 54, (1988).
- 106
Schmitt, H. D., Puzicha, M. & Gallwitz, D. Cell 53, 635–647 (1988).
- 107
Haubruck, H., Prange, R., Vorgias, C. & Gallwitz, D. EMBO J. 8, 1427–1432 (1989).
- 108
Goud, B., Salminen, A., Walworth, N. C. & Novick, P. J. Cell 53, 753–768 (1988).
- 109
Salminen, A. & Novick, P. J. J. Cell Biol. 109, 1023–1036 (1989).
- 110
Chavrier, P., Parton, R. G., Hauri, H. P., Simons, K. & Zerial, M. Cell 62, 317–329 (1990).
- 111
Connolly, T. & Gilmore, R. Cell 57, 599–610 (1989).
- 112
Dholakia, J. N. & Wahba, A. J. J. biol. Chem. 264, 546–550 (1989).
- 113
Wessling-Resnick, M. & Johnson, G. L. J. biol. Chem. 262, 12444–12447 (1987).
- 114
Wessling-Resnick, M. & Johnson, G. L. J. biol. Chem. 262, 3697–3705 (1987).
- 115
Hingorani, V. N., Tobias, D. T., Henderson, J. T. & Ho, Y. K. J. biol. Chem. 263, 6916–8926 (1988).
- 116
Reed, R. R. Cell 60, 1–2 (1990).
- 117
Fischer V. et al. Proc. natn. Acad. Sci. U.S.A. 87, 1988–1992 (1990).
- 118
Kim, S., Kikuchi, A., Mizoguchi, A. & Takai, Y. Molec. Brain Res. 6, 167–176 (1989).
- 119
Mizoguchi, A. et al. J. biol. Chem. 265, 11872–11879 (1990).
- 120
Darchen, F. et al. Proc. natn. Acad. Sci. U.S.A. 87, 5692–5696 (1990).
- 121
Sekine, A., Fujiwara, M. & Narumiya, S. J. biol. Chem. 264, 8602–8605 (1989).
- 122
Didsbury, J., Weber, R. F., Bokoch, G. M., Evans, T. & Snyderman, R. J. biol. Chem. 264, 16378–16382 (1989).
- 123
Chardin, P. et al. EMBO J. 8, 1087–1092 (1989).
- 124
Kikuchi, A., Yamamoto, K., Fujita, T. & Takai, Y. J. biol. Chem. 263, 16303–16308 (1988).
- 125
Bender, A. & Pringle, J. R. Proc. natn. Acad. Sci. U.S.A. 86, 9976–9980 (1989).
- 126
Johnson, D. I. & Pringle, J. R. J. Cell Biol. (in the press).
- 127
Sewell, J. L. & Kahn, R. A. Proc. natn. Acad. Sci. U.S.A. 85, 4620–4624 (1988).
- 128
Kahn, R. A. & Gilman, A. G. J. biol. Chem. 261, 7906–7911 (1986).
- 129
Sanders, D. A. Cell Growth Diff. 1, 251–258 (1990).
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Bourne, H., Sanders, D. & McCormick, F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125–132 (1990). https://doi.org/10.1038/348125a0
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