ArticleBiophysical journal2010
The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- The self-oscillation paradox in the flight motor ofJournal of the Royal Society, Interface · 2023Article
- Alternative N-terminal regions ofThe Journal of biological chemistry · 2020Article
- The load dependence of muscle's force-velocity curve is modulated by alternative myosin converter domains.American journal of physiology. Cell physiology · 2019Article
- 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
- Functional significance of C-terminal mobile domain of cardiac troponin I.Archives of biochemistry and biophysics · 2017Article
- An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight.The Journal of experimental biology · 2014Article
- An embryonic myosin isoform enables stretch activation and cyclical power in Drosophila jump muscle.Biophysical journal · 2013Article
- Calcium signalling indicates bilateral power balancing in the Drosophila flight muscle during manoeuvring flight.Journal of the Royal Society, Interface · 2013Article
- Conformational changes at the nucleotide site in the presence of bound ADP do not set the velocity of fast Drosophila myosins.Journal of muscle research and cell motility · 2013Article
- Article
- Alternative relay and converter domains tune native muscle myosin isoform function in Drosophila.Journal of molecular biology · 2012Article
- Calcium and stretch activation modulate power generation in Drosophila flight muscle.Biophysical journal · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We are investigating the influence of the converter and relay domains on elementary rate constants of the actomyosin cross-bridge cycle. The converter and relay domains vary between Drosophila myosin heavy chain isoforms due to alternative mRNA splicing. Previously, we found that separate insertions of embryonic myosin isoform (EMB) versions of these domains into the indirect flight muscle (IFM) myosin isoform (IFI) both decreased Drosophila IFM power and slowed muscle kinetics. To determine cross-bridge mechanisms behind the changes, we employed sinusoidal analysis while varying phosphate and MgATP concentrations in skinned Drosophila IFM fibers. Based on a six-state cross-bridge model, the EMB converter decreased myosin rate constants associated with actin attachment and work production, k(4), but increased rates related to cross-bridge detachment and work absorption, k(2). In contrast, the EMB relay domain had little influence on kinetics, because only k(4) decreased. The main alteration was mechanical, in that work production amplitude decreased. That both domains decreased k(4) supports the hypothesis that these domains are critical to lever-arm-mediated force generation. Neither domain significantly influenced MgATP affinity. Our modeling suggests the converter domain is responsible for the difference in rate-limiting cross-bridge steps between EMB and IFI myosin--i.e., a myosin isomerization associated with MgADP release for EMB and Pi release for IFI.
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