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Tropomyosin pp 73-84 | Cite as

Dimerization of Tropomyosins

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

Abstract

Tropomyosins consist of nearly 100% α-helix and assemble into parallel dimeric coiled-coils. Nonmuscle as well as muscle tropomyosins can form homodimers, however, expression of both muscle α and β tropomyosin subunits results in the preferential formation of stable α/β heterodimers in native muscle. The assembly preference of the muscle tropomyosin heterodimer can be understood in terms of its thermodynamically favorable energy distribution that provides increased stability over the homodimer. The simultaneous expression of multiple tropomyosin isoforms in nonmuscle cells (at least up to seven individual chains), however, points towards a more complex principle for determining dimer preference. The information for homoand hetero dimerization is contained within the tropomyosin molecule itself and the parameters for dimer selectivity are conferred in part by the alternatively spliced exons. However, it remains to be established if low molecular weight tropomyosin isoforms in nonmuscle cells engage in both homdimer and heterodimer formation in vivo. A thorough understanding of the selective dimer formation of the more than 40 tropomyosin isoforms is required to explain how subtle alterations in the sequence of one tropomyosin chain can result in the progression of diverse disease phenotypes.

Keywords

Coiled Coil Actin Binding Heptad Repeat Nemaline Myopathy 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.

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Copyright information

© Landes Bioscience and Springer Science+Business Media 2008

Authors and Affiliations

  • Mario Gimona
    • 1
  1. 1.Unit of Actin Cytoskeleton Regulation, Consorzio Mario Negri SudDepartment of Cell Biology and OncologySanta Maria ImbaroItaly

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