Skip to main content

Actin Filaments

  • Chapter
  • 33 Accesses

Part of the book series: Macmillan Molecular Biology Series

Abstract

Actin, the most abundant protein of the cytoskeleton, is very highly conserved, with only small differences in sequence between the polypeptides produced, for example, by slime moulds and man.1,6 This suggests that all parts of the globular actin monomer are involved in absolutely essential cellular functions. The 43 kD monomers of all types of actin assemble into filaments with a very precise structure, which has also remained constant throughout the evolution of eukaryotes.

This is a preview of subscription content, log in via an institution.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Further reading

Reviews

  1. Pollard, T. D. & Cooper, J. A. (1986). Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55, 987–1035.

    Article  CAS  PubMed  Google Scholar 

  2. Hambly, B. D., Barden, J. A., Miki, M. & dos Remedios, C. G. (1986). Structural and functional domains on actin. Bioessays 4, 124–128.

    Article  CAS  PubMed  Google Scholar 

  3. Frieden, C. (1985). Actin and tubulin polymerization. Annu. Rev. Biophys. Biophys. Chem. 14, 189–210.

    Article  CAS  PubMed  Google Scholar 

  4. Egelman, E. H. (1985). The structure of the actin thin filament. J. Muscle Res. 0026 Cell Motil. 6, 129–151.

    Article  CAS  Google Scholar 

  5. Oosawa, F. (1983). Macromolecular assembly of actin. In Muscle and Non-Muscle Motility, vol. I, pp. 151–152. New York: Academic Press.

    Chapter  Google Scholar 

  6. Korn, E. D. (1982). Actin polymerization and its regulation by proteins from nonmuscle cells. Physiol. Rev. 62, 672–737.

    CAS  PubMed  Google Scholar 

  7. Cooper, J. A. (1987). Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105, 1473–1478. (Mini-review.)

    Article  CAS  PubMed  Google Scholar 

  8. Cleveland, D. W. (1982). Treadmilling of tubulin and actin. Cell 28, 689–691. (Out of date for tubulin, but still appropriate for actin.)

    Article  CAS  PubMed  Google Scholar 

  9. Neuhaus, J.-M., Wanger, M., Keiser, T. & Wegner, A. (1983). Treadmilling of actin. J. Muscle Res. & Cell Motil. 4, 507–527.

    Article  CAS  PubMed  Google Scholar 

  10. Carlier, M.-F. (1989). Role of nucleotide hydrolysis in the dynamics of actin filaments and microtubules. Int. Rev. Cytol. 115, 139–170.

    Article  CAS  PubMed  Google Scholar 

  11. Sheterline, P. (1983). Mechanisms of Cell Motility. London & New York: Academic Press.

    Google Scholar 

  12. Oosawa, F. & Asakura, S. (1975). Thermodynamics of the polymerization of proteins. New York: Academic Press.

    Google Scholar 

Additional references

  1. Egelman, E. H., Francis, N. & DeRosier, D. J. (1982). F-actin is a helix with a random variable twist. Nature 298, 131–135.

    Article  CAS  PubMed  Google Scholar 

  2. Bullitt, E. S. A., DeRosier, D. J., Coluccio, L. M. & Tilney, L. G. (1988). Three-dimensional reconstruction of an actin bundle. J. Cell. Biol. 107, 597–611.

    Article  CAS  PubMed  Google Scholar 

  3. Schutt, C. E., Lindberg, U., Myslik, J. & Strauss, N. (1989). Molecular packing in profilin:actin crystals and its implications. J. Mol. Biol. 209, 735–746.

    Article  CAS  PubMed  Google Scholar 

  4. Suck, D., Kabsch, W. & Mannherz, G. (1981). Three-dimensional structure of the complex of skeletal muscle actin and bovine pancreatic DNase I at 6 A resolution. Proc. Natl. Acad. Sci., USA 78, 4319–4323.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Aebi, U., Fowler, W. E., Isenberg, G., Pollard, T. D. & Smith, P. R. (1981). Crystalline actin sheets: their structure and polymorphism. J. Cell Biol. 91, 340–351.

    Article  CAS  PubMed  Google Scholar 

  6. Pollard, T. D. (1986). Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103, 2747–2754.

    Article  CAS  PubMed  Google Scholar 

  7. Taylor, K. A., Reedy, M. C., Cordova, L. & Reedy, M. K. (1984). Three-dimensional reconstruction of rigor insect flight muscle from tilted thin sections. Nature 310, 285–291.

    Article  CAS  PubMed  Google Scholar 

  8. Bonder, E. M., Fishkind, D. J. & Mooseker, M. S. (1983). Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell 34, 491–501.

    Article  CAS  PubMed  Google Scholar 

  9. Korn, E. D., Carlier, M.-F. & Pantaloni, D. (1987). Actin polymerization and ATP hydrolysis. Science 238, 638–644.

    Article  CAS  PubMed  Google Scholar 

  10. Otey, C. A., Kalnoski, M. H. & Bulinski, J. C. (1987). Identification and quantification of actin isoforms in vertebrate cells and tissues. J. Cell Biochem. 34, 113–124.

    Article  CAS  PubMed  Google Scholar 

  11. Bertrand, R., Chaussepied, P., Kassab, R., Boyer, M., Benjamin, Y. & Roustan, C. (1987). Cross-linking of the skeletal myosin subfragment-1 heavy chain to the NH2-terminal region of actin within residues 40–113. J. Muscle Res. & Cell Motil. 8, 70.

    Google Scholar 

  12. Gaertner, A., Ruhnau, K., Schroer, E., Selve, N., Wanger, M.& Wegner, A. (1989). Probing nucleation, cutting and capping of actin filaments. J. Muscle Res. & Cell Motil. 10, 1–9.

    Article  CAS  Google Scholar 

  13. Millonig, R., Salvo, H. & Aebi, U. (1988). Probing actin polymerization by intermolecular crosslinking. J. Cell Biol. 106, 785–796.

    Article  CAS  PubMed  Google Scholar 

  14. Amos, L. A. (1985). Structure of muscle filaments studied by electron microscopy. Annu. Rev. Biophys. Biophys. Chem. 14, 291–314.

    Article  CAS  PubMed  Google Scholar 

  15. Taylor, K. A. & Amos, L. A. (1981). A new geometry for the geometry of the binding of myosin crossbridges to muscle thin filaments. J. Mol. Biol. 147, 297–324.

    Article  CAS  PubMed  Google Scholar 

Late additions

  1. Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F. & Holmes, K. C. (1990). Atomic structure of the actin:DNase I complex. Nature 347, 37–44.

    Article  CAS  PubMed  Google Scholar 

  2. Holmes, K. C., Popp, D., Gebhard, W. & Kabsch, W. (1990). Atomic model of the actin filament. Nature 347, 44–49.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Copyright information

© 1991 L. A. Amos and W. B. Amos

About this chapter

Cite this chapter

Amos, L.A., Amos, W.B. (1991). Actin Filaments. In: Molecules of the Cytoskeleton. Macmillan Molecular Biology Series. Palgrave, London. https://doi.org/10.1007/978-1-349-21739-7_3

Download citation

Publish with us

Policies and ethics