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

Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

5.2K
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...
5.2K
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

5.1K
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,...
5.1K
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

8.9K
Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
8.9K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

16.9K
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...
16.9K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.4K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
3.4K
Role of Myosin in Cell Migration01:18

Role of Myosin in Cell Migration

2.6K
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....
2.6K

You might also read

Related Articles

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

Sort by
Same author

Phosphate release from myosin Va occurs after the initial powerstroke but before the secondary powerstroke associated with ADP-release.

The Journal of biological chemistry·2026
Same author

Hearts may grow concentrically to balance ATP supply and demand and eccentrically to stabilize titin-based stress.

bioRxiv : the preprint server for biology·2026
Same author

Impact of salt concentration and free magnesium on human beta-cardiac myosin reveal important details about the conserved mechanochemical mechanism.

The Journal of biological chemistry·2026
Same author

Cryo-EM reveals how cardiomyopathy therapeutic drugs modulate the myosin motors of the heart.

Science advances·2026
Same author

"QuickStainer": a rapid negative staining device for improved preservation of molecular structure.

Journal of structural biology·2026
Same author

Cryo-EM Reveals How Cardiomyopathy Therapeutic Drugs Modulate the Myosin Motors of the Heart.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Oct 29, 2025

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

1.5K

A dynamic Dab2 keeps myosin VI stably on track.

Joseph A Cirilo1, Christopher M Yengo1

  • 1Department of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, Pennsylvania, USA.

The Journal of Biological Chemistry
|July 9, 2021
PubMed
Summary

Myosin VI motor proteins can transport cargo through the cell by forming transient complexes with adaptor proteins. This allows for efficient movement without disrupting the actin cytoskeleton.

Keywords:
DAB2DNA origamiFRETactinadaptor proteinclathrincytoskeletonendocytosismyosinsingle molecule

More Related Videos

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

6.2K
Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease
09:17

Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease

Published on: August 23, 2024

684

Related Experiment Videos

Last Updated: Oct 29, 2025

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

1.5K
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

6.2K
Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease
09:17

Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease

Published on: August 23, 2024

684

Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Motors

Background:

  • Myosins are essential actin-based motor proteins involved in cellular mechanical tasks.
  • Myosin transporters often form complexes with adaptors and membranes, obscuring their transport mechanisms within the actin network.

Purpose of the Study:

  • To investigate the mechanism of cargo transport by myosin VI-Dab2 complexes.
  • To determine how myosin VI facilitates processive transport without disrupting the actin cytoskeleton.

Main Methods:

  • Single-molecule kinetics
  • Förster Resonance Energy Transfer (FRET)
  • DNA origami scaffolds mimicking motor-adaptor complexes

Main Results:

  • The myosin VI-Dab2 complex exhibits weak binding and rapid turnover.
  • This dynamic interaction enables processive cargo transport.
  • Cytoskeletal integrity is maintained during myosin VI-mediated transport.

Conclusions:

  • The weak, transient nature of the myosin VI-Dab2 complex is key to its transport efficiency.
  • Myosin VI can achieve processive movement without causing major actin network disruption.
  • This study provides insights into the mechanics of intracellular transport by motor proteins.