From skeletal muscle to cancer: insights learned elucidating the function of tropomyosin

J Struct Biol. 2012 Jan;177(1):63-9. doi: 10.1016/j.jsb.2011.11.016. Epub 2011 Nov 18.

Abstract

The tropomyosins (Tms) are a family of actin filament binding proteins that possess a simple dimeric α-helical coiled-coil structure along their entire length. Our knowledge of Tm structure and function has greatly expanded since they were first discovered in skeletal muscle almost 65 years ago. In multicellular organisms they exhibit extensive cell type specific isoform diversity. In this essay we discuss the genetic mechanisms by which this diversity is generated and its significance to actin-based cellular functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / chemistry
  • Actins / metabolism
  • Animals
  • Cell Movement / drug effects
  • Endocytosis
  • Gene Expression Regulation
  • Humans
  • Muscle, Skeletal / chemistry*
  • Neoplasms / metabolism
  • Protein Binding
  • Protein Isoforms / metabolism*
  • Protein Structure, Secondary
  • Tropomyosin / metabolism*

Substances

  • Actins
  • Protein Isoforms
  • Tropomyosin