ArticleBiophysical journal2006
Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- The self-oscillation paradox in the flight motor ofJournal of the Royal Society, Interface · 2023Article
- Evolution of Flight Muscle Contractility and Energetic Efficiency.Frontiers in physiology · 2020Review
- Five Alternative Myosin Converter Domains Influence Muscle Power, Stretch Activation, and Kinetics.Biophysical journal · 2018Article
- COOH-terminal truncation of flightin decreases myofilament lattice organization, cross-bridge binding, and power output in Drosophila indirect flight muscle.American journal of physiology. Cell physiology · 2011Article
- Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Journal of biomedicine & biotechnology · 2010Review
- Removal of the cardiac myosin regulatory light chain increases isometric force production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Article
- Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.Biophysical journal · 2009Article
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length.Journal of molecular biology · 2007Article
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Authors and funding
7 authors at 3 institutions in 1 country.
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Abstract
High passive stiffness is one of the characteristic properties of the asynchronous indirect flight muscle (IFM) found in many insects like Drosophila. To evaluate the effects of two thick filament protein domains on passive sarcomeric stiffness, and to investigate their correlation with IFM function, we used microfabricated cantilevers and a high resolution imaging system to study the passive IFM myofibril stiffness of two groups of transgenic Drosophila lines. One group (hinge-switch mutants) had a portion of the endogenous S2 hinge region replaced by an embryonic version; the other group (paramyosin mutants) had one or more putative phosphorylation sites near the N-terminus of paramyosin disabled. Both transgenic groups showed severely compromised flight ability. In this study, we found no difference (compared to the control) in passive elastic modulus in the hinge-switch group, but a 15% reduction in the paramyosin mutants. All results were corroborated by muscle fiber mechanics experiments performed on the same lines. The fact that myofibril elasticity is unaffected by hinge switching implies alternative S2 hinges do not critically affect passive sarcomere stiffness. In contrast, the mechanical defects observed upon disrupting paramyosin phosphorylation sites in Drosophila suggests that paramyosin phosphorylation is important for maintaining high passive stiffness in IFM myofibrils, probably by affecting paramyosin's interaction with other sarcomeric proteins.
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