Abstract
From X-ray diffraction patterns the interfilament distances of native and reconstituted actin bundles, and of purified actin gels subjected to a range of g forces by centrifugation, have been obtained and compared. The results suggest that bundling proteins, such as villin or fimbrin, cross-link actin filaments around a minimum distance probably set by electrostatic repulsion.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Matsudaira, P. T. & Burgess, D. R. J. Cell Biol. 92, 657–664 (1982).
Mooseker, M. S. & Tilney, L. G. J. Cell Biol. 67, 725–743 (1975).
Bretscher, A. & Weber, K. Expl Cell Res. 116, 397–407 (1978).
Matsudaira, P. T. & Burgess, D. R. J. Cell Biol. 83, 667–673 (1979).
Bretscher, A. & Weber, K. Cell 20, 839–847 (1980).
Howe, C. L., Mooseker, M. S. & Graves, T. A. J. Cell Biol. 85, 916–923 (1980).
Glenney, J. R. & Weber, K. J. biol. Chem. 255, 10551–10554 (1980).
Mooseker, M. S., Graves, T. A., Wharton, K. A., Falco, N. & Howe, C. L. J. Cell Biol. 87, 809–822 (1980).
Matsudaira, P. T. & Burgess, D. R. J. Cell Biol. 92, 648–656 (1982).
Glenney, J. R., Kaulfus, P., Matsudaira, P. & Weber, K. J. biol. Chem. 256, 9283–9288 (1981).
Bretscher, A. Proc. natn. Acad. Sci. U.S.A. 78, 6849–6853 (1982).
Hanson, J. Nature 213, 353–356 (1967).
Moore, P. B., Huxley, H. E. & DeRosier, D. J. J. molec. Biol. 50, 279–295 (1970).
O'Brien, E. J., Bennett, P. M. & Hanson, J. Phil. Trans. R. Soc. B261, 201–208 (1971).
O'Brien, E. J., Giilis, J. M. & Couch, J. J. molec. Biol. 99, 461–475 (1975).
Gillis, J. M. & O'Brien, E. J. J. molec. Biol. 99, 445–459 (1975).
DeRosier, D., Mandelkow, E., Silliman, A., Tilney, L. G. & Kane, R. E. J. molec. Biol. 113, 679–695 (1977).
Spudich, J. A. & Amos, L. A. J. molec. Biol. 129, 319–331 (1979).
Tilney, L. G., DeRosier, D. J. & Mulroy, M. J. J. Cell Biol. 86, 244–259 (1980).
DeRosier, D. & Censullo, R. J. molec. Biol. 146, 77–99 (1981).
Reedy, M. K. J. molec. Biol. 31, 155–176 (1968).
Small, J. V. & Squire, J. M. J. molec. Biol. 67, 117–149 (1972).
Hanson, J., Lednev, V., O'Brien, E. J. & Bennett, P. M. Cold Spring Harb. Symp. quant. Biol. 37, 311–318 (1972).
Hanson, J. Proc. R. Soc. B183, 39–58 (1973).
Selby, C. & Bear, R. S. J. biophys. Biochem. Cytol. 3, 71–85 (1956).
Cohen, C. & Hanson, J. Biochim. biophys. Acta. 21, 177–178 (1956).
Hanson, J. Q. Rev. Biophys. 1, 177–216 (1968).
Lednev, V. V. Biofizika 19, 116–121 (1974).
Vazina, A., Frank, G. & Lemazhikhin, B. J. molec. Biol. 14, 373–380 (1965).
Spencer, M. Nature 223, 1361–1362 (1969).
Bernal, J. D. & Fankuchen, I. J. gen. Physiol. 25, 111–165 (1941).
Huxley, H. E. & Brown, W. J. molec. Biol. 30, 383–434 (1967).
Marvin, D. A., Wiseman, R. L. & Wachtel, E. J. J. molec. Biol. 82, 121–138 (1974).
Oster, G. & Riley, D. P. Acta crystallogr. 5, 272–276 (1952).
Millman, B. M. & Nickel, B. G. Biophys. J. 32, 49–63 (1980).
Franklin, R. & Klug, A. Biochim. biophys. Acta 19, 403–416 (1956).
Vibert, P. J., Haselgrove, J. C., Lowy, J. & Poulsen, F. R. J. molec. Biol. 71, 757–767 (1972).
Parry, D. A. D. & Squire, J. M. J. molec. Biol. 75, 33–55 (1973).
Haselgrove, J. C. Cold Spring Harb. Symp. quant. Biol. 37, 341–352 (1972).
Miller, A. & Treagear, R. J. molec. Biol. 70, 85–104 (1972).
Onsager, L. Ann. N.Y. Acad. Sci. 51, 627–659 (1949).
Spudich, J. A. & Watt, S. J. biol. Chem. 246, 4866–4871 (1971).
Harmsen, A. thesis, Heidelberg Univ. (1980).
Gregory, J. & Holmes, K. C. J. molec. Biol. 13, 796–801 (1965).
Suck, D., Kabsch, W. & Mannherz, H. G. Proc. natn. Acad. Sci. U.S.A. 78, 4310–4323 (1981).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Matsudaira, P., Mandelkow, E., Renner, W. et al. Role of fimbrin and villin in determining the interfilament distances of actin bundles. Nature 301, 209–214 (1983). https://doi.org/10.1038/301209a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/301209a0
This article is cited by
-
Internal motions of actin characterized by quasielastic neutron scattering
European Biophysics Journal (2011)
-
An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation
Nature Structural Biology (1998)
-
Cytoskeleton organization and submembranous interactions in intestinal and renal brush borders
Kidney International (1988)
-
Villin as a structural marker to study the assembly of the brush border
Protoplasma (1988)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.