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| The function of elastic proteins in the oscillatory contraction of insect flight muscle |
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| Author(s): Bullard B (Bullard, Belinda), Burkart C (Burkart, Christoph), Labeit S (Labeit, Siegfried), Leonard K (Leonard, Kevin) |
| Source: JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY Volume: 26 Issue: 6-8 Pages: 479-485 Published: DEC 2005 |
| Times Cited: 5 References: 29 |
| 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. |
| Document Type: Proceedings Paper |
| Language: English |
| Reprint Address: Bullard, B (reprint author), European Mol Biol Lab, D-69117 Heidelberg, Germany |
Addresses:
1. European Mol Biol Lab, D-69117 Heidelberg, Germany
2. Univ Klinikum Mannheim, Inst Anasthesiol & Operat Intens Med, D-68135 Mannheim, Germany
3. Univ York, Dept Biol, York YO10 5DD, N Yorkshire England |
| Publisher: SPRINGER, VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS |
| Subject Category: Cell Biology |
| IDS Number: 059DI |
| ISSN: 0142-4319 |
| DOI: 10.1007/s10974-005-9032-7 |
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