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

Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

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 homology) domains...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...

You might also read

Related Articles

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

Sort by
Same author

Ancient enzymes, new biotechnology applications.

Nature reviews. Molecular cell biology·2026
Same author

Mechanically Programmable DNA Hydrogel Microparticles for 3D Cellular Systems.

Advanced materials (Deerfield Beach, Fla.)·2026
Same author

Fibrillar adhesion dynamics govern the timescales of nuclear mechano-response via the vimentin cytoskeleton.

Nature materials·2026
Same author

Guidance of cellular nematic elastomers into shape-programmable living surfaces.

Science (New York, N.Y.)·2026
Same author

Exploring the binding properties and activities of ancestral expansins.

International journal of biological macromolecules·2026
Same author

Targeting the Akt-EphA2 axis and cell-cell adhesion enhances anoikis sensitivity in cancer cells.

Scientific reports·2026

Related Experiment Video

Updated: Jun 26, 2026

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
08:28

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques

Published on: November 2, 2018

Stretching single talin rod molecules activates vinculin binding.

Armando del Rio1, Raul Perez-Jimenez, Ruchuan Liu

  • 1Department of Biological Sciences, Columbia University, New York, NY 10027, USA.

Science (New York, N.Y.)
|January 31, 2009
PubMed
Summary

Mechanical stretching of single proteins like talin can expose hidden binding sites, activating molecular interactions. This reveals a new mechanism for how cells sense and respond to physical forces.

More Related Videos

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

Related Experiment Videos

Last Updated: Jun 26, 2026

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
08:28

Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques

Published on: November 2, 2018

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

Area of Science:

  • Biophysics
  • Cell Biology
  • Molecular Mechanobiology

Background:

  • The precise molecular mechanisms translating mechanical stimuli into cellular chemical responses remain largely unknown.
  • Understanding mechanotransduction is crucial for deciphering cellular signaling and tissue organization.

Purpose of the Study:

  • To elucidate the molecular mechanism of force transduction in the talin-vinculin interaction.
  • To investigate how mechanical force affects protein structure and binding interactions.

Main Methods:

  • Utilized single-molecule techniques including magnetic tweezers, total internal reflection fluorescence (TIRF), and atomic force microscopy (AFM).
  • Applied physiologically relevant forces to individual talin protein rods.

Main Results:

  • Mechanical stretching of single talin rods exposed previously hidden (cryptic) binding sites.
  • This force-induced exposure of binding sites facilitated vinculin binding to talin.
  • Demonstrated that talin stretching activates vinculin binding, initiating downstream signaling.

Conclusions:

  • Molecular mechanotransduction can occur via the exposure of buried binding sites upon protein stretching.
  • The talin-vinculin system exemplifies a mechanism where force directly alters protein conformation to mediate binding.
  • Protein stretching-induced binding site exposure may represent a general principle in biological force transduction.