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

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...
Cytoskeletal Coordination in Cell Migration01:32

Cytoskeletal Coordination in Cell Migration

A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...
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.
Cell Motility through Blebbing01:16

Cell Motility through Blebbing

Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
In multicellular...
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,...
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

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 cargos...

You might also read

Related Articles

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

Sort by
Same author

A song of heads and tails: myosin II conformational regulation and filament dynamics shape force generation in non-muscle cells.

Biophysical reviews·2026
Same author

MYH9 mutations differentially stabilize non-muscle myosin II filaments and induce distinct cellular aggregation phenotypes.

Cellular and molecular life sciences : CMLS·2026
Same author

Molecular Control of Non-Muscle Myosin II-A Aggregation and Intracellular Dynamics by motor- or tail-specific <i>MYH9</i> Mutations.

bioRxiv : the preprint server for biology·2025
Same author

Role of c-ABL in DENV-2 Infection and Actin Remodeling in Vero Cells.

International journal of molecular sciences·2025
Same author

Characterization of the Temporal Dynamics of the Endothelial-Mesenchymal-like Transition Induced by Soluble Factors from Dengue Virus Infection in Microvascular Endothelial Cells.

International journal of molecular sciences·2025
Same author

Sos1 ablation alters focal adhesion dynamics and increases Mmp2/9-dependent gelatinase activity in primary mouse embryonic fibroblasts.

Cell communication and signaling : CCS·2025

Related Experiment Video

Updated: May 15, 2026

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

Cell migration: cooperation between myosin II isoforms in durotaxis.

Miguel Vicente-Manzanares1, Miguel Vicente Manzanares

  • 1Ramón y Cajal Program, Universidad Autonoma de Madrid School of Medicine, Servicio de Inmunología, Hospital Universitario de la Princesa, Madrid, Spain. miguel.vicente@uam.es

Current Biology : CB
|January 12, 2013
PubMed
Summary

Non-muscle myosin II is crucial for mesenchymal stem cell durotaxis. Both II-A and II-B isoforms work together, but II-A serine phosphorylation hinders this movement.

More Related Videos

A Cell-based Assay to Investigate Non-muscle Myosin II Contractility via the Folded-gastrulation Signaling Pathway in Drosophila S2R+ Cells
07:15

A Cell-based Assay to Investigate Non-muscle Myosin II Contractility via the Folded-gastrulation Signaling Pathway in Drosophila S2R+ Cells

Published on: August 19, 2018

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
12:35

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

Related Experiment Videos

Last Updated: May 15, 2026

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

A Cell-based Assay to Investigate Non-muscle Myosin II Contractility via the Folded-gastrulation Signaling Pathway in Drosophila S2R+ Cells
07:15

A Cell-based Assay to Investigate Non-muscle Myosin II Contractility via the Folded-gastrulation Signaling Pathway in Drosophila S2R+ Cells

Published on: August 19, 2018

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
12:35

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

Area of Science:

  • Cell Biology
  • Biophysics
  • Stem Cell Research

Background:

  • Mesenchymal stem cells (MSCs) are vital for tissue regeneration.
  • Cell migration on substrates with varying stiffness (durotaxis) is a key biological process.
  • The molecular mechanisms governing MSC durotaxis are not fully understood.

Purpose of the Study:

  • To investigate the role of non-muscle myosin II (NMII) in MSC durotaxis.
  • To identify the specific NMII isoforms involved and their functions.
  • To explore the regulatory mechanisms, such as phosphorylation, affecting NMII in durotaxis.

Main Methods:

  • Utilized live-cell imaging and traction force microscopy to observe MSC behavior on defined stiffness gradients.
  • Employed small molecule inhibitors and genetic knockdown strategies to target NMII isoforms (NMII-A and NMII-B).
  • Performed Western blotting and site-directed mutagenesis to analyze the phosphorylation status of NMII-A.

Main Results:

  • NMII is essential for MSCs to migrate up stiffness gradients.
  • Both NMII-A and NMII-B are cooperatively required for efficient durotaxis.
  • Serine phosphorylation of NMII-A was found to inhibit its contribution to durotaxis.

Conclusions:

  • Non-muscle myosin II isoforms, particularly NMII-A and NMII-B, are critical regulators of mesenchymal stem cell durotaxis.
  • The interplay between NMII isoforms and post-translational modifications like serine phosphorylation dictates cell migration responses to substrate stiffness.
  • These findings provide new insights into the biophysical mechanisms controlling stem cell behavior and potential therapeutic targets.