Abstract
The protein oligomer forming the gap junction channel has been analysed in two Ca2+-sensitive states by electron microscopy of membranes in frozen aqueous solutions. Switching between states occurs by a small cooperative rearrangement involving tilting of the subunits, which may be responsible for the effect of Ca2+ on channel permeability in vivo.
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References
Rose, B. & Loewenstein, W. R. Nature 254, 250–252 (1975).
Spray, D. C., Stern, J. H., Harris, A. L. & Bennett, M. V. L. Proc. natn. Acad. Sci. U.S.A. 79, 441–445 (1981).
Makowski, L., Caspar, D. L. D., Phillips, W. C. & Goodenough, D. A. J. Cell Biol. 74, 629–645 (1977).
Unwin, P. N. T. & Zampighi, G. Nature 283, 545–549 (1980).
Hertzberg, E. G., Lawrence, T. S. & Gilula, N. B. A. Rev. Physiol. 43, 479–491 (1981).
Loewenstein, W. R. Physiol. Rev. 61, 829–913 (1981).
Unwin, P. N. T. & Ennis, P. D. J. Cell Biol. 97, 1459–1466 (1983).
Taylor, K. A. & Glaeser, R. M. Science 186, 1036–1037 (1974).
Dubochet, J., Lepault, J., Freeman, R., Berriman, J. A. & Homo, J.-C. J. Microsc. 128, 219–237 (1982).
Henderson, R. & Unwin, P. N. T. Nature 257, 28–32 (1975).
Agard, D. A. J. molec. Biol. 167, 849–852 (1983).
Caspar, D. L. D., Goodenough, D. A., Makowski, L. & Phillips, W. C. J. Cell Biol. 74, 605–628 (1977).
Hertzberg, E. L. & Gilula, N. B. J. biol. Chem. 254, 2138–2147 (1979).
Nicholson, B. J., Hunkapiller, M. W., Grim, L. B., Hood, L. E. & Revel, J.-P. Proc. natn. Acad. Sci. U.S.A. 78, 7594–7598 (1981).
Flagg-Newton, J., Simpson, I. & Loewenstein, W. R. Science 205, 404–407 (1979).
Schwarzmann, G. et al. Science 213, 551–553 (1981).
Durham, A. C. H. & Klug, A. Nature new Biol. 229, 6–10 (1971).
Robinson, I. K. & Harrison, S. C. Nature 297, 563–568 (1982).
Thon, F. Z. Naturforsch. 219, 476–478 (1966).
Jaffe, J. & Glaeser, R. M. Proc. 40th an. EMSA Meet., 72–73 (San Francisco, (1982).
Taylor, K. A., Milligan, R. A., Raeburn, C. & Unwin, P. N. T. Ultramicroscopy (submitted).
Unwin, P. N. T. & Henderson, R. J. molec. Biol. 95, 425–440 (1975).
Baker, T. S., Caspar, D. L. D., Hollingshead, C. J. & Goodenough, D. A. J. Cell Biol. 96, 204–216 (1983).
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Unwin, P., Ennis, P. Two configurations of a channel-forming membrane protein. Nature 307, 609–613 (1984). https://doi.org/10.1038/307609a0
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DOI: https://doi.org/10.1038/307609a0
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