ArticleBiophysical journal2012
A branched kinetic scheme describes the mechanochemical coupling of Myosin Va processivity in response to substrate.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- Myosin V: Chemomechanical-coupling ratchet with load-induced mechanical slip.Scientific reports · 2017Article
- Flexural Stiffness of Myosin Va Subdomains as Measured from Tethered Particle Motion.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2015Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Myosin Va is a double-headed cargo-carrying molecular motor that moves processively along cellular actin filaments. Long processive runs are achieved through mechanical coordination between the two heads of myosin Va, which keeps their ATPase cycles out of phase, preventing both heads detaching from actin simultaneously. The biochemical kinetics underlying processivity are still uncertain. Here we attempt to define the biochemical pathways populated by myosin Va by examining the velocity, processive run-length, and individual steps of a Qdot-labeled myosin Va in various substrate conditions (i.e., changes in ATP, ADP, and P(i)) under zero load in the single-molecule total internal reflection fluorescence microscopy assay. These data were used to globally constrain a branched kinetic scheme that was necessary to fit the dependences of velocity and run-length on substrate conditions. Based on this model, myosin Va can be biased along a given pathway by changes in substrate concentrations. This has uncovered states not normally sampled by the motor, and suggests that every transition involving substrate binding and release may be strain-dependent.
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Registered trials
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