ArticleProceedings of the National Academy of Sciences of the United States of America2006
An exceptionally fast actomyosin reaction powers insect flight muscle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 64 citations in OpenAlex.
- Stage-Specific Proteomic Adaptations to Heme-Induced Oxidative Stress inInternational journal of molecular sciences · 2026Article
- Causal models of rate-independent damping in insect exoskeleta.The Journal of experimental biology · 2025Article
- A Drosophila cardiac myosin increases jump muscle stretch activation and shortening deactivation.Biophysical journal · 2025Article
- Myosin dilated cardiomyopathy mutation S532P disrupts actomyosin interactions, leading to altered muscle kinetics, reduced locomotion, and cardiac dilation inMolecular biology of the cell · 2021Article
- Prolonged myosin binding increases muscle stiffness in Drosophila models of Freeman-Sheldon syndrome.Biophysical journal · 2021Article
- Alternative N-terminal regions ofThe Journal of biological chemistry · 2020Article
- CryoEM structure ofLife science alliance · 2020Article
- The load dependence of muscle's force-velocity curve is modulated by alternative myosin converter domains.American journal of physiology. Cell physiology · 2019Article
- The R249Q hypertrophic cardiomyopathy myosin mutation decreases contractility in Drosophila by impeding force production.The Journal of physiology · 2019Article
- Molecular parallelism in fast-twitch muscle proteins in echolocating mammals.Science advances · 2018Article
- Article
- Five Alternative Myosin Converter Domains Influence Muscle Power, Stretch Activation, and Kinetics.Biophysical journal · 2018Article
- Stretch activation properties of Drosophila and Lethocerus indirect flight muscle suggest similar calcium-dependent mechanisms.American journal of physiology. Cell physiology · 2017Article
- ADisease models & mechanisms · 2017Article
- Flightin maintains myofilament lattice organization required for optimal flight power and courtship song quality inProceedings. Biological sciences · 2017Article
- The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type.American journal of physiology. Cell physiology · 2017Article
- Structure of myosin filaments from relaxedScience advances · 2016Article
- An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight.The Journal of experimental biology · 2014Article
- Mutations of the Drosophila myosin regulatory light chain affect courtship song and reduce reproductive success.PloS one · 2014Article
- X-ray diffraction from flight muscle with a headless myosin mutation: implications for interpreting reflection patterns.Frontiers in physiology · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Insects, as a group, have been remarkably successful in adapting to a great range of physical and biological environments, in large part because of their ability to fly. The evolution of flight in small insects was accompanied by striking adaptations of the thoracic musculature that enabled very high wing beat frequencies. At the cellular and protein filament level, a stretch activation mechanism evolved that allowed high-oscillatory work to be achieved at very high frequencies as contraction and nerve stimulus became asynchronous. At the molecular level, critical adaptations occurred within the motor protein myosin II, because its elementary interactions with actin set the speed of sarcomere contraction. Here, we show that the key myosin enzymatic adaptations required for powering the very fast flight muscles in the fruit fly Drosophila melanogaster include the highest measured detachment rate of myosin from actin (forward rate constant, 3,698 s(-1)), an exceptionally weak affinity of MgATP for myosin (association constant, 0.2 mM(-1)), and a unique rate-limiting step in the cross-bridge cycle at the point of inorganic phosphate release. The latter adaptations are constraints imposed by the overriding requirement for exceptionally fast release of the hydrolytic product MgADP. Otherwise, as in Drosophila embryonic muscle and other slow muscle types, a step associated with MgADP release limits muscle contraction speed by delaying the detachment of myosin from actin.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.