Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Actin and Myosin in Muscle Contraction01:16

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...
Cross-bridge Cycle01:26

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.
Role of Myosin in Cell Migration01:18

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. It is...
Overview of Myosin Structure and Function01:15

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 characterized.
Excitation-Contraction Coupling in Skeletal Muscles01:20

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 potential...
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

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,...

You might also read

Related Articles

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

Sort by
Same author

Dynamic switching of cell-substrate contact sites allows gliding diatoms to modulate the curvature of their paths.

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

Intellectual disability-causing mutations in KIF11 impair microtubule dynamics and dendritic arborization.

Nature communications·2026
Same author

Kinesin-Induced Buckling Reveals the Limits of Microtubule Self-Repair.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Microtubule lattice defects facilitate spastin-mediated severing.

Journal of cell science·2026
Same author

Lowering Ionic Strength Improves the Sensitivity of Microtubule Gliding Assay Based Molecular Detection.

Nano letters·2025
Same author

Microscope-Free Analyte Detection Based on Fiber-Optic Gliding Motility Assays.

Small (Weinheim an der Bergstrasse, Germany)·2025
Same journal

Near-exceptional point degeneracy enables multilevel optical memory.

Nature nanotechnology·2026
Same journal

Monolithic manufacturing of an electrically addressable quasi-suspended nanophotonic aperture.

Nature nanotechnology·2026
Same journal

Halide-site-substituting spacer creates quasi-two-dimensional perovskites for vapour-deposited light-emitting diodes.

Nature nanotechnology·2026
Same journal

Nanoscale amorphization of poly(triarylamine) for efficient and stable inverted perovskite photovoltaics.

Nature nanotechnology·2026
Same journal

Bridging nanotechnology and mechanobiology.

Nature nanotechnology·2026
Same journal

Coherent 2D/3D van der Waals epitaxy enables single-crystal perovskite heterostructures.

Nature nanotechnology·2026
See all related articles

Related Experiment Video

Updated: May 23, 2026

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
09:38

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

Published on: July 1, 2021

Myosin shifts into reverse gear

Wilhelm J Walter, Stefan Diez

    Nature Nanotechnology
    |April 7, 2012
    PubMed
    Summary

    No abstract available in PubMed .

    More Related Videos

    Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
    06:53

    Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

    Published on: May 4, 2022

    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
    08:57

    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

    Published on: February 4, 2021

    Related Experiment Videos

    Last Updated: May 23, 2026

    Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
    09:38

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

    Published on: July 1, 2021

    Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
    06:53

    Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers

    Published on: May 4, 2022

    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
    08:57

    Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

    Published on: February 4, 2021