Letter | Published:

Binding of ATP to tubulin

Nature volume 296, pages 775776 (22 April 1982) | Download Citation

Subjects

Abstract

Microtubules are present in all eukaryotic cells and participate in a variety of cellular processes1. From recent studies it has become clear that nucleotides have a central role in the assembly of tubulin into microtubules2–5. The tubulin dimer binds two moles of guanine nucleotide: one (at the E-site) which can exchange with exogenous nucleotide and one (at the N-site) which does not exchange6. E-site GTP is hydrolysed during the assembly process4,7,8. Microtubule assembly can be induced by ATP through a contaminating nucleoside diphosphokinase activity that regenerates GTP following its hydrolysis—this is associated with tubulin polymerization4,9,10. Recent reports suggest that ATP has other effects on the assembly kinetics11–13, and we have shown14,15, using tubulin preparations lacking the nucleoside diphosphokinase activity, that ATP may play a critical part in the regulation of microtubule formation by binding to tubulin at a site which is distinct from the N- and E-sites. Kinetic data suggest a model in which ATP can act at the level of nucleation to stimulate assembly15. We now report the first direct evidence for the binding of ATP to tubulin and show that the corresponding dissociation constant is in a range of physiological significance.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1.

    Roberts, K. & Hyams, J. S. (eds) Microtubules (Academic, New York, 1979).

  2. 2.

    Science 177, 1104–1105 (1972).

  3. 3.

    , & J. molec. Biol 89, 455–468 (1974).

  4. 4.

    & J. molec. Biol. 115, 643–673 (1977).

  5. 5.

    , & Biochemistry 15, 4248–4254 (1976).

  6. 6.

    , & Biochemistry 7, 4466–4479 (1968).

  7. 7.

    J. Biochem, Tokyo 77, 1193–1197 (1975).

  8. 8.

    , & Proc. natn. Acad. Sci. U.S.A. 74, 5372–5376 (1977).

  9. 9.

    & Biochem. biophys. Res. Commun. 68 (1976); Proc. natn. Acad. Sci. U.S.A. 74, 5372–5376 (1976).

  10. 10.

    & J. biol. Chem. 253, 1984–1990 (1978)

  11. 11.

    Brain Res. 172, 382–386 (1979).

  12. 12.

    & Cell 18, 673–679 (1979).

  13. 13.

    , & J. Biochem, Tokyo 85, 495–502, 127–135 (1979).

  14. 14.

    & J. biol Chem. 255, 11981–11985 (1980).

  15. 15.

    & J. biol. Chem. (in the press).

  16. 16.

    & Biochim. biophys. Acta 63, 530–532 (1962).

  17. 17.

    & Biochemistry 18, 3880–3886 (1979).

  18. 18.

    & Archs Biochem. Biophys. 203, 404–411 (1980).

  19. 19.

    & in Methods of Enzymatic Analysis (ed. Bergmeyer, H. U.) 2266–2302 (Academic, New York, 1974).

  20. 20.

    , , & J. biol. Chem. 193, 265–275 (1951).

Download references

Author information

Affiliations

  1. Department of Biochemistry, University of California, Berkeley, California 94720, USA

    • James R. Zabrecky
    •  & R. David Cole

Authors

  1. Search for James R. Zabrecky in:

  2. Search for R. David Cole in:

About this article

Publication history

Received

Accepted

Published

DOI

https://doi.org/10.1038/296775a0

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.