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Related Concept Videos

The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
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Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
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Cross-bridge Cycle01:26

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As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
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The Movement of Organelles and Vesicles01:43

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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
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Updated: May 16, 2025

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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Microscale velocity-dependent unbinding generates a macroscale performance-efficiency tradeoff in actomyosin systems.

Jake McGrath1, Brian Kent1,2, Colin L Johnson1

  • 1Center for Nonlinear Dynamics, Department of Physics, University of Texas at Austin, Austin, Texas, USA.

Communications Biology
|May 12, 2025
PubMed
Summary
This summary is machine-generated.

Myosin motor detachment rate (α) impacts cellular energy use. Muscle-like models reveal this nonlinearity balances power and efficiency, optimizing biological and robotic actuators.

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Area of Science:

  • Biophysics
  • Cellular mechanics
  • Robotics

Background:

  • Myosin motors are essential ATP-powered biological machines.
  • The link between myosin detachment rate and cellular energy dynamics is not fully understood.
  • Existing models connect myosin velocity to muscle dynamics but not energetics.

Purpose of the Study:

  • To develop a model linking myosin unbinding (α) to cellular energetics.
  • To experimentally validate the performance-efficiency tradeoff governed by α.
  • To investigate the role of nonlinearity in muscle efficiency.

Main Methods:

  • Developed an analytical model relating myosin unbinding parameter α to energetics.
  • Constructed HillBot, a robophysical Hill muscle model, to decouple α's effects.
  • Analyzed 136 published α measurements from in-vivo muscle samples.

Main Results:

  • The analytical model aligns with in-vivo muscle data, showing a performance-efficiency tradeoff.
  • HillBot demonstrated that nonlinearity significantly influences muscle efficiency.
  • A distribution of α values in muscle samples was identified (α* = 3.85 ± 2.32).

Conclusions:

  • Myosin's nonlinearity (α) is crucial for balancing power and efficiency in biological actuators.
  • The observed α* in muscle represents a generalist actuator strategy.
  • Insights can inform nonlinear variable-impedance control for robotics.