ArticleProceedings of the National Academy of Sciences of the United States of America2004
Repriming the actomyosin crossbridge cycle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Recent insights into the relative timing of myosin's powerstroke and release of phosphate.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Altered cross-bridge properties in skeletal muscle dystrophies.Frontiers in physiology · 2014Review
- Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.Biophysical journal · 2013Article
- Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Biophysical journal · 2012Article
- Mechanism of regulation of native cardiac muscle thin filaments by rigor cardiac myosin-S1 and calcium.The Journal of biological chemistry · 2010Article
- Phosphorylation of cardiac troponin I at protein kinase C site threonine 144 depresses cooperative activation of thin filaments.The Journal of biological chemistry · 2010Article
- A strain-dependency of Myosin off-rate must be sensitive to frequency to predict the B-process of sinusoidal analysis.Advances in experimental medicine and biology · 2010Article
- Effect of low pH on single skeletal muscle myosin mechanics and kinetics.American journal of physiology. Cell physiology · 2008Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The central features of the mechanical cycle that drives the contraction of muscle are two translational steps: the working stroke, whereby an attached myosin crossbridge moves relative to the actin filament, and the repriming step, in which the crossbridge returns to its original orientation. Although the mechanism of the first of these is understood in some detail, that of the second has received less attention. Here, we show that repriming occurs after detachment of the crossbridge from the actin, rather than intervening between two actomyosin states with ATP bound [Eisenberg, E. & Greene, L. E. (1980) Annu. Rev. Physiol. 42, 293-309]. To discriminate between these two models we investigated the single-molecule mechanics of the myosin-actin interaction in the presence of ATP analogues such as GTP, for which the hydrolytic step itself limits the actomyosin GTPase rate to a much lower rate than for ATP. The lifetimes of bound states was proportional to 1/[GTP], indicating that during the bound period myosin was in the actomyosin rigor configuration. Moreover, despite the very low actomyosin GTPase, the rate of actin binding and formation of the rigor state was higher than with ATP; it follows that most interactions with actin result in the release of GTP and not of the products, GDP and phosphate. There was no significant movement of the actin during this interaction, so repriming must occur while myosin is dissociated, as in the original Lymn-Taylor scheme [Lymn, R. W. & Taylor, E. W. (1971) Biochemistry 10, 4617-4624].
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