Journal of Muscle Research & Cell Motility

, Volume 26, Issue 6, pp 479–485

The function of elastic proteins in the oscillatory contraction of insect flight muscle

  • Belinda Bullard
  • Christoph Burkart
  • Siegfried Labeit
  • Kevin Leonard
Article

DOI: 10.1007/s10974-005-9032-7

Cite this article as:
Bullard, B., Burkart, C., Labeit, S. et al. J Muscle Res Cell Motil (2005) 26: 479. doi:10.1007/s10974-005-9032-7

Abstract

Oscillatory contraction of asynchronous insect flight muscle is activated by periodic stretches at constant low concentrations of Ca2+. The fibres must be relatively stiff to respond to small length changes occurring at high frequency. Several proteins in the flight muscle may determine the overall stiffness of the fibres. The Drosophila sallimus (sls) gene codes for multiple isoforms with a modular structure made up of immunoglobulin (Ig) and elastic PEVK domains, unique sequence, and a few fibronectin (Fn) domains at the end of the molecule. Kettin, derived from the sls gene, has Ig domains separated by linker sequences and is bound to actin near the Z-disc; the C-terminus is associated with the end of the A-band. Flight muscle also has longer isoforms of Sls, with extensible PEVK sequence, and C-terminal Fn domains; all extend from the Z-disc to the end of the A-band. Projectin, from a different gene, has repeating modules of Fn and Ig domains, and is associated with the end of thick filaments; tandem Ig and PEVK domains at the N-terminus are in the I-band. Projectin, kettin and other Sls isoforms form a mechanical link between thick and thin filaments; all are probably part of the connecting filaments, which branch from the thick filaments and are linked to actin near the Z-disc. The elasticity of fibres may depend on the relative amounts of those isoforms with extensible PEVK sequence. Flightin is bound on the outside of thick filaments and maintains the stiffness necessary for the transmission of stress along the filaments. Insect flight muscle has multiple elastic proteins to give the sarcomere the optimum compliance necessary for high frequency oscillatory contraction.

Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  • Belinda Bullard
    • 1
    • 3
  • Christoph Burkart
    • 2
  • Siegfried Labeit
    • 2
  • Kevin Leonard
    • 1
  1. 1.European Molecular Biology LaboratoryHeidelbergGermany
  2. 2.Institut für Anästhesiologie und Operative IntensivmedizinUniversitätsklinikumMannheimGermany
  3. 3.Department of BiologyUniversity of YorkYorkUK