Regulating the contraction of insect flight muscle

The rapid movement of the wings in small insects is powered by the indirect flight muscles. These muscles are capable of contracting at up to 1,000 Hz because they are activated mechanically by stretching. The mechanism is so efficient that it is also used in larger insects like the waterbug, Lethocerus. The oscillatory activity of the muscles occurs a low concentration of Ca(2+), which stays constant as the muscles contract and relax. Activation by stretch requires particular isoforms of tropomyosin and the troponin complex on the thin filament. We compare the tropomyosin and troponin of Lethocerus and Drosophila with that of vertebrates. The characteristics of the flight muscle regulatory proteins suggest ways in which stretch-activation works. There is evidence for bridges between troponin on thin filaments and myosin crossbridges on the thick filaments. Recent X-ray fibre diffraction results suggest that a pull on the bridges activates the thin filament by shifting tropomyosin from a blocking position on actin. The troponin bridges are likely to contain extended sequences of tropomyosin or troponin I (TnI). Flight muscle has two isoforms of TnC with different Ca(2+)-binding properties: F1 TnC is needed for stretch-activation and F2 TnC for isometric contractions. In this review, we describe the structural changes in both isoforms on binding Ca(2+) and TnI, and discuss how the steric model of muscle regulation can apply to insect flight muscle.