Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Role of Myosin in Cell Migration

Role of Myosin in Cell Migration

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.
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....

Actin and Myosin in Muscle Contraction

Actin and Myosin in Muscle Contraction

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...

Overview of Myosin Structure and Function

Overview of Myosin Structure and Function

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...

Excitation-Contraction Coupling in Skeletal Muscles

Excitation-Contraction Coupling in Skeletal Muscles

Excitation-contraction coupling is a series of events that occur between generating an action potential and initiating a muscle contraction. It occurs at the triad, a structure found in skeletal muscle fibers that comprise a T-tubule and terminal cisternae of the sarcoplasmic reticulum on each side. These triads are visible in longitudinally sectioned muscle fibers. They are typically located at the A-I junction — the junction between the A and I bands of the sarcomere.
When an action...

Mechanical Protein Functions

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.

Cross-bridge Cycle

Cross-bridge Cycle

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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A local solution to local load: Myo1E as a tension-responsive actuator in clathrin-mediated endocytosis.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Non-muscle tropomyosins inhibit myosin-19 and dynamically localize to mitochondrially associated actin filaments.

The Journal of biological chemistry·2026

Same author

DACIT device for axon cancer cell interaction testing in 2D and 3D.

iScience·2026

Same author

Protocol for fabrication and utilization of the device for axon-cancer cell interaction testing.

STAR protocols·2025

Same author

A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachment.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

S2Tag, a novel affinity tag for the capture and immobilization of coiled-coil proteins: Application to the study of human β-cardiac myosin.

The Journal of biological chemistry·2025

Search research articles

Related Experiment Video

Updated: Mar 21, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Force Generation by Membrane-Associated Myosin-I.

Serapion Pyrpassopoulos¹, Göker Arpağ², Elizabeth A Feeser¹

¹The Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine at the University of Pennsylvania, Philadelphia PA 19104-6085, USA.

Scientific Reports

|May 10, 2016

Summary

Vertebrate myosin-IC (Myo1c) generates force parallel to cell membranes by interacting with actin filaments and lipid bilayers. Its force generation is enhanced when it operates away from the membrane plane or in slower-diffusing membrane regions.

More Related Videos

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

Published on: July 1, 2021

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Published on: July 12, 2022

Related Experiment Videos

Last Updated: Mar 21, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

Published on: May 4, 2022

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy

Published on: July 1, 2021

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Published on: July 12, 2022

Area of Science:

Cell biology
Biophysics
Molecular motors

Background:

Vertebrate myosin-IC (Myo1c) is a type-1 myosin crucial for linking cell membranes to the cytoskeleton.
It possesses an actin-binding motor domain and a phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2)-binding tail domain.
Previous studies showed Myo1c propels actin filaments in fluid bilayers but its force-generating capacity against load was unexplored.

Purpose of the Study:

To investigate the force-generating capabilities of membrane-bound Myo1c against external load.
To measure the diffusion coefficient of single membrane-bound Myo1c molecules.
To explore how Myo1c ensembles develop and sustain forces while interacting with fluid lipid bilayers.

Main Methods:

Utilized optical tweezers for force-relaxation experiments to measure single Myo1c diffusion.
Assessed the force development and sustainability by ensembles of membrane-bound Myo1c.
Developed a computational model to interpret experimental data on Myo1c force generation.

Main Results:

Single membrane-bound Myo1c molecules' diffusion coefficients were measured.
Ensembles of Myo1c demonstrated the ability to develop and sustain forces.
Computational modeling indicated Myo1c ensembles generate forces parallel to lipid bilayers.

Conclusions:

Myosin-IC ensembles can generate forces parallel to lipid bilayers.
Force generation is optimized when Myo1c operates away from the membrane plane.
Anchoring to slowly diffusing membrane regions enhances Myo1c force generation.