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Updated: Oct 16, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Direct observation of processive movement by individual myosin V molecules
T Sakamoto1, I Amitani, E Yokota
1Department of Physics, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa-ken, 920-1192, Japan.
Abstract:
Myosin V is an unconventional myosin thought to move processively along actin filaments. To have hard evidence for the high processivity, we sought to observe directly the movement by individual native chick brain myosin V (BMV) molecules with fluorescent calmodulin. Single BMV molecules did exhibit highly processive movement along actin filaments fixed to a coverslip. BMV continued to move up to the barbed end of its actin track, and did not readily detach from action. The barbed end, therefore, got brighter with time, because of a constant stream of BMV traffic. The maximum speed of the processive movement was 1 microm/s, and the maximum actin-activated ATPase rate was 2.4 s(-1). These values apparently imply that BMV travels a great distance, 400 nm, per an ATPase cycle.
Insights
Individual chick brain myosin V (BMV) molecules demonstrated highly processive movement along actin filaments. This provides direct evidence for BMV
Area of Science:
- Molecular Biology
- Cell Biology
- Biophysics
Background:
- Myosin V is an unconventional myosin implicated in intracellular transport.
- Previous studies suggested high processivity, but direct observation was lacking.
Purpose of the Study:
- To provide direct evidence for the high processivity of native chick brain myosin V (BMV) molecules.
- To characterize the movement dynamics of individual BMV molecules.
Main Methods:
- Utilized single-molecule imaging of fluorescently labeled native chick brain myosin V (BMV).
- Observed BMV interaction with actin filaments immobilized on a coverslip.
Main Results:
- Individual BMV molecules exhibited highly processive movement along actin filaments.
- BMV moved processively towards the barbed end of actin, with minimal detachment.
- Observed maximum speeds of 1 microm/s and actin-activated ATPase rates of 2.4 s(-1).
Conclusions:
- Direct observation confirms the highly processive nature of BMV.
- BMV likely travels approximately 400 nm per ATPase cycle, supporting its role in long-range transport.
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