Biochemistry and Regulation of Nonmuscle Actins

Toward an Understanding of Cell Motility and Shape Determination
  • Dennis G. Uyemura
  • James A. Spudich
Part of the Biological Regulation and Development book series (BRD, volume 2)


Actin is a component of virtually all eukaryotic cells. In cells of many types, it is the most abundant protein species. Moreover, many of its physical and chemical properties have been absolutely conserved throughout evolution. These observations underscore the critical nature of the contractile and cytoskeletal functions ascribed to actin. It is essential, therefore, in understanding cell motility and shape determination to address the regulation of actin polymerization, the intracellular distribution of actin, and the interaction of actin with myosin. It is the thesis of this chapter that substantial further insights into the regulation of actin in nonmuscle cells can be obtained only by a multifaceted approach involving biochemical, ultrastructural, and genetic techniques. Of course, the single common denominator in all such studies is actin itself. Hence, such studies can be built only on a solid foundation: a broad, quantitative characterization of actin purified from each organism selected for study.


Muscle Actin Thin Filament Dictyostelium Discoideum Acanthamoeba Castellanii Nonmuscle Cell 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Abramowitz, J. W., Stracher, A., and Detwiler, T. C., 1975, A second form of actin: Platelet microfilaments depolymerized by ATP and divalent cations, Arch. Biochem. Biophys. 167:230–237.PubMedCrossRefGoogle Scholar
  2. Adelman, M. R., 1977, Physarum actin. Observation on its presence, stability, and assembly in plasmodial extracts and development of an improved purification procedure, Biochemistry 16:4862–4871.PubMedCrossRefGoogle Scholar
  3. Blikstad, I., Markey, F., Carlson, L., Persson, T., and Lindberg, U., 1978, Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I, Cell 15:935–943.PubMedCrossRefGoogle Scholar
  4. Boxer, L. A., and Stossel, T. P., 1975, Isolation and interactions of contractile proteins from chronic myelogenous leukemia granulocytes (CMLG), J. Cell Biol. 67:40a.Google Scholar
  5. Bray, D., and Thomas, C., 1976, Unpolymerized actin in fibroblasts and brain, J. Mol. Biol. 105:527–544.PubMedCrossRefGoogle Scholar
  6. Brown, S. S., and Spudich, J. A., 1979, Nucleation of polar actin filament assembly by a positively-charged surface, J. Cell Biol. 80:499–504.PubMedCrossRefGoogle Scholar
  7. Bryan, J., and Kane, R. E., 1978, Separation and interaction of the components of sea urchin actin gel, J. Mol. Biol. 125:207–224.PubMedCrossRefGoogle Scholar
  8. Carlsson, L., Nyström, L.-E., Lindberg, U., Kannan, K. K., Cid-Dresdner, H., Lövgren, S., and Jörnvall, H., 1976a, Crystallization of a non-muscle actin, J. Mol. Biol. 105:353–366.PubMedCrossRefGoogle Scholar
  9. Carlsson, L., Nyström, L.-E., Sundkvist, I., Markey, F., and Lindberg, U., 1976b, Profilin, a low-molecular weight protein controlling actin polymerizability, in: Contractile Systems in Nonmuscle Tissues (S. V. Perry, A. Margreth, and R. S. Adelstein, eds.), pp. 39–49, Elsevier North-Holland Biomedical Press, Amsterdam.Google Scholar
  10. Carlsson, L., Nyström, L.-E., Sundkvist, I., Markey, F., and Lindberg, U., 1977, Actin polymerizability is influenced by profilin, a low molecular weight protein in nonmuscle cells, J. Mol. Biol. 115:465–483.PubMedCrossRefGoogle Scholar
  11. Clarke, M., 1978, A selection method for isolating motility mutants of Dictyostelium discoideum, in: Cell Reproduction: Daniel Mazia Dedicatory Volume (R. E. Dirkson, D. Prescott, and C. F. Fox, eds.), pp. 621–629, Academic Press, New York.Google Scholar
  12. Clarke, M., and Spudich, J. A., 1977, Nonmuscle contractile proteins: The role of actin and myosin in cell motility and shape determination, Annu. Rev. Biochem. 46:797–822.PubMedCrossRefGoogle Scholar
  13. Collins, J. H., and Elzinga, M., 1975, The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence, J. Biol. Chem. 250:5915–5920.PubMedGoogle Scholar
  14. Cooke, R., 1975, The role of the bound nucleotide in the polymerization of actin, Biochemistry 14:3250–3256.PubMedCrossRefGoogle Scholar
  15. Depue, R. H., Jr., and Rice, R. V., 1965, F-actin is a right-handed helix, J. Mol. Biol. 12:302–303.PubMedCrossRefGoogle Scholar
  16. DeRosier, D., Mandelkow, E., Silliman, A., Tilney, L., and Kane, R., 1977, Structure of actin-containing filaments from two types of nonmuscle cells, J. Mol. Biol. 113:679–695.PubMedCrossRefGoogle Scholar
  17. Elzinga, M., and Lu, R. C., 1976, Comparative amino acid sequence studies on actins, in: Contractile Systems in Nonmuscle Tissues (S. V. Perry, A. Margreth, and R. S. Adelstein, eds.), pp. 29–37, Elsevier NorthHolland Biomedical Press, Amsterdam.Google Scholar
  18. Elzinga, M., Maron, B. J., and Adelstein, R. S., 1976, Human heart and platelet actins are products of different genes, Science 191:94–95.PubMedCrossRefGoogle Scholar
  19. Engel, J., Fasold, H., Hulla, F. W., Waechter, F., and Wegner, A., 1977, The polymerization reaction of muscle actin, Mol. Cell. Biochem. 18:3–14.PubMedCrossRefGoogle Scholar
  20. Garrels, J. I., and Gibson, W., 1976, Identification and characterization of multiple forms of actin, Cell 9:793–805.PubMedCrossRefGoogle Scholar
  21. Goldman, R., Pollard, T., and Rosenbaum, J. (eds.), 1976, Cell Motility, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.Google Scholar
  22. Gordon, D. J., Eisenberg, E., and Korn, E. D., 1976a, Characterization of cytoplasmic actin isolated from Acanthamoeba castellanii by a new method, J. Biol. Chem. 251:4778–4786.PubMedGoogle Scholar
  23. Gordon, D. J., Yang, Y. Z., and Korn, E. D., 1976b, Polymerization of Acanthamoeba actin. Kinetics, thermodynamics, and co-polymerization with muscle actin, J. Biol. Chem. 251:7474–7479.PubMedGoogle Scholar
  24. Gordon, D. J., Boyer, J., and Korn, E. D., 1977, Comparative biochemistry of nonmuscle actins, J. Biol. Chem. 252:8300–8309.PubMedGoogle Scholar
  25. Hardy, M. F., and Perry, S. V., 1969, In vitro methylation of muscle proteins, Nature (London) 223:300–302.CrossRefGoogle Scholar
  26. Hardy, M. F., Harris, C. I., Perry, S. V., and Stone, D., 1970, Occurrence and formation of the Ne-methyllysines in myosin and the myofibrillar proteins, Biochem. J. 120:653–660.PubMedGoogle Scholar
  27. Hartwig, J. H., and Stossel, T. P., 1975, Isolation and properties of actin, myosin, and a new actin-binding protein in rabbit alveolar macrophages, J. Biol. Chem. 250:5696–5705.PubMedGoogle Scholar
  28. Hatano, S., and Owaribe, K., 1977, A simple method for the isolation of actin from myxomycete plasmodia, J. Biochem. 82:201–205.PubMedGoogle Scholar
  29. Heggeness, M. H., Wang, K., and Singer, S. J., 1977, Intracellular distributions of mechanochemical proteins in cultured fibroblasts, Proc. Natl. Acad. Sci. U.S.A. 74:3883–3887.PubMedCrossRefGoogle Scholar
  30. Hitchcock, S. E., 1977, Regulation of motility in nonmuscle cells, J. Cell Biol. 74:1–15.PubMedCrossRefGoogle Scholar
  31. Huxley, H. E., 1973, Structural changes in the actin- and myosin-containing filaments during contraction, Cold Spring Harbor Symp. Quant. Biol. 37:361–376.CrossRefGoogle Scholar
  32. Kane, R. E., 1975, Preparation and purification of polymerized actin from sea urchin egg extracts, J. Cell. Biol. 66:305–315.PubMedCrossRefGoogle Scholar
  33. Kane, R. E., 1976, Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts, J. Cell Biol. 71:704–714.PubMedCrossRefGoogle Scholar
  34. Korn, E. D., 1978, Biochemistry of actomyosin-dependent cell motility (a review), Proc. Natl. Acad. Sci. U.S.A. 75:588–599.PubMedCrossRefGoogle Scholar
  35. Krzysik, B., Vergnes, J. P., and McManus, I. R., 1971, Enzymatic methylation of skeletal muscle contractile proteins, Arch. Biochem. Biophys. 146:34–45.PubMedCrossRefGoogle Scholar
  36. Lazarides, E., and Lindberg, U., 1974, Actin is the naturally occurring inhibitor of deoxyribonuclease I, Proc. Natl. Acad. Sci. U.S.A. 71:4742–4746.PubMedCrossRefGoogle Scholar
  37. Lu, R. C., and Elzinga, M., 1977, Partial amino acid sequence of brain actin and its homology with muscle actin, Biochemistry 16:5801–5806.PubMedCrossRefGoogle Scholar
  38. Mannherz, H. G., Kabsch, W., and Leberman, R., 1977, Crystals of skeletal muscle actin: Pancreatic DNAase I complex, FEBS Lett 73:141–143.PubMedCrossRefGoogle Scholar
  39. Maruta, H., and Korn, E. D., 1977, Purification from Acanthamoeba castellanii of proteins that induce gelation and syneresis of F-actin, J. Biol. Chem. 252:399–402.PubMedGoogle Scholar
  40. Oosawa, F., and Asakura, S., 1975, Thermodynamics of the Polymerization of Protein, Academic Press, London.Google Scholar
  41. Paik, W. K., and Kim, S., 1975, Protein methylation: Chemical, enzymological, and biological significance, Adv. Enzymol. 42:227–286.PubMedGoogle Scholar
  42. Pardee, J. D., and Bamburg, J. R., 1979, Actin from embryonic chick brain. Isolation in high yield and comparison of biochemical properties with chicken muscle actin, Biochemistry 18:2245–2252.PubMedCrossRefGoogle Scholar
  43. Pollard, T. D., 1976, Cytoskeletal functions of cytoplasmic contractile proteins, J. Supramol. Struct. 5:317–334.PubMedCrossRefGoogle Scholar
  44. Pollard, T. D., and Weihing, R. R., 1974, Actin and myosin and cell movement, CRC Crit. Rev. Biochem. 2:1–65.PubMedCrossRefGoogle Scholar
  45. Pollard, T. D., Fujiwara, K., Niederman, R., and Maupin-Szamier, P., 1976, Evidence for the role of cytoplasmic actin and myosin in cellular structure and motility, in: Cell Motility (R. Goldman, T. Pollard, and J. Rosenbaum, eds.), pp. 689–724, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y,Google Scholar
  46. Rubenstein, P. A., and Spudich, J. A., 1977, Actin microheterogeneity in chick embryo fibroblasts, Proc. Natl. Acad. Sci. U.S.A. 74:120–123.PubMedCrossRefGoogle Scholar
  47. Schachat, F. H., Harris, H. E., and Epstein, H. F., 1978, Actin from the nematode, Caenorhabditis elegans, is a single electrofocusing species, Biochim. Biophys. Acta 493:304–309.Google Scholar
  48. Shizuta, Y., Shizuta, H., Gallo, M., Davies, P., Pastan, I., and Lewis, M. S., 1976, Purification and properties of filamin. an actin binding protein from chicken gizzard, J. Biol. Chem. 251:6562–6567.PubMedGoogle Scholar
  49. Spudich, J. A., and Cooke, R., 1975, Supramolecular forms of actin from amoebae of Dictyostelium discoideum, J. Biol. Chem. 250:7485–7491.PubMedGoogle Scholar
  50. Spudich, J. A., Huxley, H. E., and Finch, J. T., 1972, Regulation of skeletal muscle contraction. II. Structural studies of the interaction of the tropomyosin-troponin complex with actin, J. Mol. Biol. 72:619–632.PubMedCrossRefGoogle Scholar
  51. Uyemura, D. G., Brown, S. S., and Spudich, J. A., 1978, Biochemical and structural characterization of actin from Dictyostelium discoideum, J. Biol. Chem. 253:9088–9096.PubMedGoogle Scholar
  52. Vandekerckhove, J., and Weber, K., 1978, Mammalian cytoplasmic actins are the product of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins, Proc. Natl. Acad. Sci. U.S.A. 75:1106–1110.PubMedCrossRefGoogle Scholar
  53. Wakabayashi, T., Huxley, H. E., Amos, L. A., and Klug, A., 1975, Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complex, J. Mol. Biol. 93:477–497.PubMedCrossRefGoogle Scholar
  54. Wang, K., 1977, Filamin, a new high-molecular-weight protein found in smooth muscle and nonmuscle cells. Purification and properties of chicken gizzard filamin, Biochemistry 16:1857–1865.PubMedCrossRefGoogle Scholar
  55. Wang, K., and Singer, S. J., 1977, Interaction of filamin with F-actin in solution, Proc. Natl. Acad. Sci. U.S.A. 74:2021–2025.PubMedCrossRefGoogle Scholar
  56. Wang, K., Ash, J. F., and Singer, S. J., 1975, Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells, Proc. Natl. Acad. Sci. U.S.A. 72:4483–4486.PubMedCrossRefGoogle Scholar
  57. Wegner, A., 1976, Head to tail polymerization of actin, J. Mol. Biol. 108:135–150.CrossRefGoogle Scholar
  58. Weihing, R. R., and Korn, E. D., 1972, Acanthamoeba actin. Composition of the peptide that contains 3methylhistidine and a peptide that contains Ne-methyllysine, Biochemistry 11:1538–1543.PubMedCrossRefGoogle Scholar
  59. Whalen, R. G., Butler-Browne, G. S., and Gros, F., 1976, Protein synthesis and actin heterogeneity in calf muscle cells in culture, Proc. Natl. Acad. Sci. U.S.A. 73:2018–2022.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • Dennis G. Uyemura
    • 1
  • James A. Spudich
    • 2
  1. 1.Department of BiochemistryState University of New YorkStony BrookUSA
  2. 2.Department of Structural Biology, Sherman Fairchild CenterStanford University School of MedicineStanfordUSA

Personalised recommendations