ArticleThe Journal of biological chemistry2011
Nanomechanics of the cadherin ectodomain: "canalization" by Ca2+ binding results in a new mechanical element.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Nanomechanics of wild-type and mutant dimers of the inner-ear tip-link protein protocadherin 15.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Nanomechanics of wild-type and mutant dimers of the tip-link protein protocadherin 15.bioRxiv : the preprint server for biology · 2023Article
- Application and underlying mechanism of acupuncture for the nerve repair after peripheral nerve injury: remodeling of nerve system.Frontiers in cellular neuroscience · 2023Review
- Elastic versus brittle mechanical responses predicted for dimeric cadherin complexes.Biophysical journal · 2022Article
- Nanomechanics of tip-link cadherins.Scientific reports · 2019Article
- Elasticity of individual protocadherin 15 molecules implicates tip links as the gating springs for hearing.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Mechanically Weak Extracellular Membrane-Adjacent Domain Induces Dimerization of Protocadherin-15.Biophysical journal · 2018Article
- Beyond Cell-Cell Adhesion: Sensational Cadherins for Hearing and Balance.Cold Spring Harbor perspectives in biology · 2018Review
- The cohesin module is a major determinant of cellulosome mechanical stability.The Journal of biological chemistry · 2018Article
- Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.Scientific reports · 2018Article
- A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15.Structure (London, England : 1993) · 2017Article
- An elastic element in the protocadherin-15 tip link of the inner ear.Nature communications · 2016Article
- Molecular Mechanoneurobiology: An Emerging Angle to Explore Neural Synaptic Functions.BioMed research international · 2015Review
- Biophysical properties of intrinsically disordered p130Cas substrate domain--implication in mechanosensing.PLoS computational biology · 2014Article
- Article
- Three functions of cadherins in cell adhesion.Current biology : CB · 2013Review
- Mechanical properties of β-catenin revealed by single-molecule experiments.Biophysical journal · 2012Article
- Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Biophysical journal · 2012Article
- Sensing sound: molecules that orchestrate mechanotransduction by hair cells.Trends in neurosciences · 2012Review
- Unequivocal single-molecule force spectroscopy of proteins by AFM using pFS vectors.Biophysical journal · 2012Article
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cadherins form a large family of calcium-dependent cell-cell adhesion receptors involved in development, morphogenesis, synaptogenesis, differentiation, and carcinogenesis through signal mechanotransduction using an adaptor complex that connects them to the cytoskeleton. However, the molecular mechanisms underlying mechanotransduction through cadherins remain unknown, although their extracellular region (ectodomain) is thought to be critical in this process. By single molecule force spectroscopy, molecular dynamics simulations, and protein engineering, here we have directly examined the nanomechanics of the C-cadherin ectodomain and found it to be strongly dependent on the calcium concentration. In the presence of calcium, the ectodomain extends through a defined ("canalized") pathway that involves two mechanical resistance elements: a mechanical clamp from the cadherin domains and a novel mechanostable component from the interdomain calcium-binding regions ("calcium rivet") that is abolished by magnesium replacement and in a mutant intended to impede calcium coordination. By contrast, in the absence of calcium, the mechanical response of the ectodomain becomes largely "decanalized" and destabilized. The cadherin ectodomain may therefore behave as a calcium-switched "mechanical antenna" with very different mechanical responses depending on calcium concentration (which would affect its mechanical integrity and force transmission capability). The versatile mechanical design of the cadherin ectodomain and its dependence on extracellular calcium facilitate a variety of mechanical responses that, we hypothesize, could influence the various adhesive properties mediated by cadherins in tissue morphogenesis, synaptic plasticity, and disease. Our work represents the first step toward the mechanical characterization of the cadherin system, opening the door to understanding the mechanical bases of its mechanotransduction.
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