The sarcomeric cytoskeleton: From molecules to motion

Mathias Gautel*, Kristina Djinović-Carugo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

152 Citations (Scopus)
298 Downloads (Pure)

Abstract

Highly ordered organisation of striated muscle is the prerequisite for the fast and unidirectional development of force and motion during heart and skeletal muscle contraction. A group of proteins, summarised as the sarcomeric cytoskeleton, is essential for the ordered assembly of actin and myosin filaments into sarcomeres, by combining architectural, mechanical and signalling functions. This review discusses recent cell biological, biophysical and structural insight into the regulated assembly of sarcomeric cytoskeleton proteins and their roles in dissipating mechanical forces in order to maintain sarcomere integrity during passive extension and active contraction. α-Actinin crosslinks in the Z-disk show a pivot-and-rod structure that anchors both titin and actin filaments. In contrast, the myosin crosslinks formed by myomesin in the M-band are of a ball-and-spring type and may be crucial in providing stable yet elastic connections during active contractions, especially eccentric exercise.

Original languageEnglish
Pages (from-to)135-145
Number of pages11
JournalJournal of Experimental Biology
Volume219
Issue number2
DOIs
Publication statusE-pub ahead of print - 20 Jan 2016

Keywords

  • Cytoskeleton
  • M-band
  • Myomesin
  • Obscurin
  • Sarcomere
  • Striated muscle
  • Titin
  • Z-disk
  • α-Actinin

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