Tropomyosin structure, function, and interactions: A dynamic regulator

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Tropomyosin is the archetypal-coiled coil, yet studies of its structure and function have proven it to be a dynamic regulator of actin filament function in muscle and non-muscle cells. Here we review aspects of its structure that deviate from canonical leucine zipper coiled coils that allow tropomyosin to bind to actin, regulate myosin, and interact directly and indirectly with actin-binding proteins. Four genes encode tropomyosins in vertebrates, with additional diversity that results from alternate promoters and alternatively spliced exons. At the same time that periodic motifs for binding actin and regulating myosin are conserved, isoform-specific domains allow for specific interaction with myosins and actin filament regulatory proteins, including troponin. Tropomyosin can be viewed as a universal regulator of the actin cytoskeleton that specifies actin filaments for cellular and intracellular functions.

Original languageEnglish (US)
Pages (from-to)253-284
Number of pages32
JournalSub-cellular biochemistry
StatePublished - Jan 1 2017

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology
  • Cancer Research


  • Actin
  • Actin cytoskeleton
  • Actin filament dynamics
  • Coiled coil
  • Myosin
  • Myosin regulation
  • Tropomyosin


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