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

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

The Role of Actin and Myosin in Non-muscle Cells

6.1K
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...
6.1K
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

4.3K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
4.3K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.5K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.5K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

31.8K
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...
31.8K
Mechanical Protein Functions01:58

Mechanical Protein Functions

5.9K
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. 
5.9K
Protein Complex Assembly02:41

Protein Complex Assembly

17.3K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
17.3K

You might also read

Related Articles

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

Sort by
Same author

In vivo reduction of Treg expansion in rodent helminth-malaria coinfection.

Parasites & vectors·2026
Same author

Total Synthesis of Photoswitchable Latrunculin B Enables Reversible Control of Actin Polymerization and Cell Migration.

Journal of the American Chemical Society·2026
Same author

A Bayesian modelling framework for estimating tick-borne pathogen transmission dynamics at the host-tick interface.

PLoS computational biology·2026
Same author

Asymmetric Phosphoinositide Lipid Bilayers Generated by Spontaneous Lipid Insertion.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Coinfection with malaria alters the fecundity and within-host persistence of an intestinal nematode.

PLoS neglected tropical diseases·2026
Same author

Actomyosin-dependent assembly of the mechanosensitive machinery from adherens junctions triggers actin polymerization and organization.

Science advances·2026

Related Experiment Video

Updated: Apr 19, 2026

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
09:10

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

Published on: August 25, 2022

4.0K

Reconstituting actomyosin-dependent mechanosensitive protein complexes in vitro.

Corina Ciobanasu1, Bruno Faivre1, Christophe Le Clainche1

  • 1Laboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique (CNRS), Gif-sur-Yvette, France.

Nature Protocols
|December 16, 2014
PubMed
Summary

Researchers developed a new in vitro assay to observe how force affects protein binding. This method visualizes the force-dependent recruitment of vinculin to talin, a key step in mechanosensitive processes.

More Related Videos

The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
08:50

The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton

Published on: March 10, 2023

1.3K
Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
11:55

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

Published on: July 12, 2022

3.0K

Related Experiment Videos

Last Updated: Apr 19, 2026

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
09:10

Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics

Published on: August 25, 2022

4.0K
The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
08:50

The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton

Published on: March 10, 2023

1.3K
Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
11:55

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

Published on: July 12, 2022

3.0K

Area of Science:

  • Cell Biology
  • Biophysics
  • Biochemistry

Background:

  • Mechanosensitive biological processes rely on actin-binding proteins (ABPs) to sense cytoskeletal forces.
  • These forces trigger ABPs to recruit effector proteins, but observing this in vitro is challenging.

Purpose of the Study:

  • To develop and describe an in vitro assay for observing force-dependent protein binding.
  • To study the actomyosin-dependent binding of vinculin to the ABP talin.

Main Methods:

  • Developed an in vitro assay using purified proteins and micropatterned surfaces.
  • Immobilized talin on disc-shaped islands and used actomyosin networks to generate force.
  • Utilized total internal reflection fluorescence (TIRF) microscopy to visualize EGFP-vinculin binding to stretched talin and Alexa Fluor 594-labeled actin.

Main Results:

  • Demonstrated the force-dependent revelation of cryptic vinculin-binding sites (VBSs) in talin upon extension.
  • Quantified vinculin binding to talin under constant force using a stable actomyosin network.
  • Measured vinculin dissociation linked to talin refolding using actomyosin cables with force application and release cycles.

Conclusions:

  • The developed assay allows for the observation of force-dependent protein interactions in vitro.
  • This method provides insights into the kinetics of vinculin-talin binding, crucial for mechanosensitive processes.
  • The protocol enables detailed study of protein recruitment in response to mechanical forces.