Letter | Published:

Fluorescence techniques for following interactions of microtubule subunits and membranes

Naturevolume 254pages152154 (1975) | Download Citation

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Abstract

THERE is increasing evidence that several cell functions are controlled by the state of polymerisation of microtubules (MTs) and by the interaction of MTs with membranes. For example, previous studies in our laboratory have shown that colchicine-sensitive structures, presumably MTs, determine the topographical organisation of cell membrane components1–3. Conditions for the polymerisation of MTs in vitro have been described4. The MT subunit has been identified by centrifugation studies as a 6S dimer of approximately 110,000 daltons5. An additional 36S component is required for MT assembly6. The established procedures used, however, to record MT polymerisation (light scattering and viscosity measurements supplemented by negative staining and electron microscopy) do not reveal details of the interactions between subunits undergoing polymerisation and cannot be applied in the presence of elements such as membranes that contribute separately to light scatter and viscosity.

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References

  1. 1

    Berlin, R. D., Oliver, J. M., Ukena, T. E., and Yin, H. H., Nature, 247 45–46 (1974).

  2. 2

    Oliver, J. M., Ukena, T. E., and Berlin, R. D., Proc. natn. Acad. Sci. U.S.A., 71 394–398 (1974).

  3. 3

    Ukena, T. E., Borysenko, J. Z., Karnovsky, M. J., and Berlin, R. D., J. Cell Biol., 61, 70–82 (1974).

  4. 4

    Weisenberg, R. C., Science, 177, 1196 (1972).

  5. 5

    Weisenberg, R. C., Borisy, G. G., and Taylor, E. W., Biochemistry, 12, 4466–4479 (1968).

  6. 6

    Kirschner, M. W., Williams, R. C., Weingarten, M., and Gerhart, J. C., Proc. natn. Acad. Sci. U.S.A., 71, 1159–1163 (1974).

  7. 7

    Forster, T. H., Disc. Faraday Soc., 27, 7–17 (1959).

  8. 8

    Wu, C-W., and Stryer, L., Proc. natn. Acad. Sci. U.S.A., 69, 1104–1108 (1972).

  9. 9

    Bunting, J. R., and Cathou, R. E., J. molec. Biol., 77, 223–235 (1973).

  10. 10

    Gennis, L. S., Gennis, R. B., and Cantor, C. R., Biochemistry, 11, 2517–2524 (1972).

  11. 11

    Shelanski, M. L., Gaskin, F., and Cantor, C. R., Proc. natn. Acad. Sci. U.S.A., 70, 765–768 (1973).

  12. 12

    Chen, R. F., Archs Biochem. Biophys., 133, 263–276 (1969).

  13. 13

    Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., J. biol. Chem., 193, 265–275 (1951).

  14. 14

    Yguerrabide, J., Methods in enzymology, 26, Part C., 498–578, (Academic, New York, 1972).

  15. 15

    Olmsted, J. B., and Borisy, G. G., Ann. Rev. Biochem., 42, 507–540 (1973).

  16. 16

    Gennis, R. B., and Cantor, C. R., Biochemistry, 11, 2509–2517 (1972).

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Affiliations

  1. Department of Physiology, Schools of Medicine and Dental Medicine, University of Connecticut, Farmington, Connecticut, 06032

    • JOEL S. BECKER
    • , JANET M. OLIVER
    •  & RICHARD D. BERLIN

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https://doi.org/10.1038/254152a0

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