ArticleBiophysical journal2014
Integrin-generated forces lead to streptavidin-biotin unbinding in cellular adhesions.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Measuring cellular force using DNA-based tension probes: from ensemble to single-molecule studies.Nature protocols · 2026Review
- Synthetic aptamer mechanoreceptors enable cell-specific force sensing and temporal control via DNA circuits.Nature communications · 2026Article
- Selective Suppression of Integrin-Ligand Binding by Single Molecular Tension Probes Mediates Directional Cell Migration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- DNA mechanocapsules for programmable piconewton responsive drug delivery.Nature communications · 2024Article
- All-Covalent Nuclease-Resistant and Hydrogel-Tethered DNA Hairpin Probes Map pN Cell Traction Forces.ACS applied materials & interfaces · 2023Article
- Production of mutant streptavidin protein and investigation of its effect on the performance of streptavidin.Iranian journal of basic medical sciences · 2023Article
- Interplay of Affinity and Surface Tethering in Protein Recognition.The journal of physical chemistry letters · 2022Article
- DNA Tension Probes Show that Cardiomyocyte Maturation Is Sensitive to the Piconewton Traction Forces Transmitted by Integrins.ACS nano · 2022Article
- Mechanotransduction in hippocampal neurons operates under localized low picoNewton forces.iScience · 2022Article
- Biophysical Approaches for Applying and Measuring Biological Forces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Molecular Tension Probes to Quantify Cell-Generated Mechanical Forces.Molecules and cells · 2022Review
- The biophysics of cancer: emerging insights from micro- and nanoscale tools.Advanced nanobiomed research · 2022Article
- Turn-key mapping of cell receptor force orientation and magnitude using a commercial structured illumination microscope.Nature communications · 2021Article
- A reversible shearing DNA probe for visualizing mechanically strong receptors in living cells.Nature cell biology · 2021Article
- Modulating mechanical stability of heterodimerization between engineered orthogonal helical domains.Nature communications · 2020Article
- Regulation and dynamics of force transmission at individual cell-matrix adhesion bonds.Science advances · 2020Article
- Forces during cellular uptake of viruses and nanoparticles at the ventral side.Nature communications · 2020Article
- Extending the Capabilities of Molecular Force Sensors via DNA Nanotechnology.Critical reviews in biomedical engineering · 2020Review
- Mechanical Regulation of Nuclear Translocation in Migratory Neurons.Frontiers in cell and developmental biology · 2020Review
- Molecular Tension Sensors: Moving Beyond Force.Current opinion in biomedical engineering · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The interplay between chemical and mechanical signals plays an important role in cell biology, and integrin receptors are the primary molecules involved in sensing and transducing external mechanical cues. We used integrin-specific probes in molecular tension fluorescence microscopy to investigate the pN forces exerted by integrin receptors in living cells. The molecular tension fluorescence microscopy probe consisted of a cyclic Arg-Gly-Asp-D-Phe-Lys(Cys) (cRGDfK(C)) peptide tethered to the terminus of a polyethylene glycol polymer that was attached to a surface through streptavidin-biotin linkage. A fluorescence resonance energy transfer mechanism was used to visualize tension-driven extension of the polymer. Surprisingly, we found that integrin receptors dissociate streptavidin-biotin tethered ligands in focal adhesions within 60 min of cell seeding. Although streptavidin-biotin binding affinity is described as the strongest noncovalent bond in nature, and is ~10(6) - 10(8) times larger than that of integrin-RGD affinity, our results suggest that individual integrin-ligand complexes undergo a marked enhancement in stability when the receptor assembles in the cell membrane. Based on the observation of streptavidin-biotin unbinding, we also conclude that the magnitude of integrin-ligand tension in focal adhesions can reach values that are at least 10 fold larger than was previously estimated using traction force microscopy-based methods.
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