ArticleJournal of muscle research and cell motility2014
Loop 2 of myosin is a force-dependent inhibitor of the rigor bond.
Article in Journal of muscle research and cell motility, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Tonotopic specialization of MYO7A isoforms in auditory hair cells.Nature communications · 2026Article
- Insights into Actin Isoform-Specific Interactions with Myosin via Computational Analysis.Molecules (Basel, Switzerland) · 2024Article
- The Force-Dependent Mechanism of an Integrin α4β7-MAdCAM-1 Interaction.International journal of molecular sciences · 2023Article
- Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Cell adhesion. The minimal cadherin-catenin complex binds to actin filaments under force.Science (New York, N.Y.) · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Myosin's actin-binding loop (loop 2) carries a charge opposite to that of its binding site on actin and is thought to play an important role in ionic interactions between the two molecules during the initial binding step. However, no subsequent role has been identified for loop 2 in actin-myosin binding. We used an optical trap to measure bond formation and bond rupture between actin and rigor heavy meromyosin when loaded perpendicular to the filament axis. We studied HMM with intact or proteolytically cleaved loop 2 at low and physiologic ionic strength. Here we show that the presence of intact loop 2 allows actomyosin bonds to form quickly and that they do so in a short-lived bound state. Increasing tensile load causes the transition to a long-lived state-the distinguishing behavior of a catch bond. When loop 2 was cleaved catch bond behavior was abrogated leaving only a long-lived state. These data suggest that in addition to its role in locating binding sites on actin, loop 2 is also a force-dependent inhibitor of the long-lived actomyosin complex. This may be important for reducing the duty ratio and increasing the shortening velocity of actomyosin at low forces.
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Registered trials
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