Introduction and Historical Perspective

  • Peter Gunning
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 644)

Abstract

Tropomyosin is a coiled coil dimer which forms a polymer along the major groove of the majority of actin filaments. It is therefore one of the two primary components of the actin filament. Our understanding of the biological function of tropomyosin has been driven almost entirely by its role in striated muscle. This reflects both its original discovery as part of the thin filament in skeletal muscle and its pivotal role in regulating muscle contraction. In contrast, its role in the function of the cytoskeleton of all cells has been poorly understood due, at least in part, to the technical challenge of deciphering the function of a large number of isoforms. This book has brought together many of the leading researchers who have defined the function of tropomyosin in both normal and pathological conditions. Each author brings their own perspective in a series of stand alone reviews of the areas of tropomyosin research they have played a major role in defining.

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References

  1. 1.
    Gunning P, O’Neill G, Hardeman E. Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol Rev 2008; 88:1–35.PubMedCrossRefGoogle Scholar
  2. 2.
    Gunning PW, Schevzov G, Kee AJ et al. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol 2005; 15(6):333–341.PubMedCrossRefGoogle Scholar
  3. 3.
    Gordon AM, Homsher E, Regnier M. Regulation of contraction instriated muscle. Physiol Rev 2000; 80:853–924.PubMedGoogle Scholar
  4. 4.
    Geeves MA, Holmes KC. The molecular mechanism of muscle contraction. Adv Protein Chem 2005: 71:161–193.PubMedCrossRefGoogle Scholar
  5. 5.
    Perry SV. Vertebrate tropomyosin: distribution, properties and function. J Muscle Res Cell Motil 2001; 22:5–49.PubMedCrossRefGoogle Scholar
  6. 6.
    Pawlak G, Helfman DM. Cytoskeletal changes in cell transformation and tumorigenesis. Curr Opin Genet Dev 2001; 11(1):41–47.PubMedCrossRefGoogle Scholar
  7. 7.
    Bailey K. Tropomyosin a new asymmetric protein of muscle. Nature 1946; 157:368.CrossRefGoogle Scholar
  8. 8.
    Bailey K. Tropomyosin: a new asymmetric protein of the muscle fibril. Biochem J 1948; 43:271–279.Google Scholar
  9. 9.
    Huxley HE. Structural changes in the actin-and myosin-containing filaments during contraction. Cold Spring Harb Symp Quant Biol 1972; 37:361–376.Google Scholar
  10. 10.
    Parry DA, Squire JM. Structural role of tropomyosin in muscle regulation: analysis of the x-ray diffraction patterns from relaxed and contracting muscles. J Mol Biol 1973; 75:33–55.PubMedCrossRefGoogle Scholar
  11. 11.
    Lander ES, Linton LM, Birren B et al. Initial sequencing and analysis of the human genome. Nature 2001; 409:860–921.PubMedCrossRefGoogle Scholar
  12. 12.
    Venter JC, Adams MD, Myers EW et al. The sequence of the human genome. Science 2001; 291:1304–1351.PubMedCrossRefGoogle Scholar
  13. 13.
    Gunning PW. Protein isoforms and isozymes. Nature Encyclopedia Human Genome 2003; 835–839.Google Scholar
  14. 14.
    Lazarides E. Tropomyosin antibody: the specific localization of tropomyosin in nonmuscle cells. J Cell Biol 1975; 65:549–561.PubMedCrossRefGoogle Scholar
  15. 15.
    Matsumura F, Lin J-J, Yamashiro-Matsumura S et al. Differential expression of tropomyosin forms in the microfilaments isolated from normal and transformed rat cultured cells J Biol Chem 1983; 258:13954–13964.PubMedGoogle Scholar
  16. 16.
    Hendricks M, Weintraub H. Multiple tropomyosin polypeptides in chicken embryo fibroblasts: differential repression of transcription by rous sarcoma virus transformation. Mol Cell Biol 1984; 4:1823–1833.PubMedGoogle Scholar
  17. 17.
    Lin JJ, Helfman DM, Hughes SH et al. Tropomyosin isoforms in chicken embryo fibroblasts: purification, characterization, changes in Rous sarcoma virus-transformed cells. J Cell Biol 1985; 100:692–703.PubMedCrossRefGoogle Scholar
  18. 18.
    Bernstein BW, Bamburg JR. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil 1982; 2:1–8.PubMedCrossRefGoogle Scholar
  19. 19.
    Broschat KO, Burgess DR. Low Mr tropomyosin isoforms from chicken brain and intestinal epithelium have distinct actin-binding properties. J Biol Chem 1986; 261:13350–13359.PubMedGoogle Scholar
  20. 20.
    Ishikawa R, Yamashiro S, Matsumura F. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. J Biol Chem 1989; 264:7490–7497.PubMedGoogle Scholar
  21. 21.
    Fanning AS, Wolenski JS, Mooseker MS et al. Differential regulation of skeletal muscle myosin-II and brush border myosin-I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cell Motil Cytoskeleton 1994; 29:29–45.PubMedCrossRefGoogle Scholar
  22. 22.
    Cooper HL. Actin dynamics: tropomyosin provides stability. Curr Biol 2002; 12:R523–R525.PubMedCrossRefGoogle Scholar
  23. 23.
    Bryce NS, Schevzov G, Ferguson V et al. Specification of actin filament function and molecular composition by tropomyosin isoforms. Mol Biol Cell 2003; 14:1002–1016.PubMedCrossRefGoogle Scholar

Copyright information

© Landes Bioscience and Springer Science+Business Media 2008

Authors and Affiliations

  • Peter Gunning
    • 1
  1. 1.Oncology Research Unit, Department of Pharmacology, School of Medical SciencesUniversity of New South WalesSydneyAustralia

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