α-Catenin cytomechanics – role in cadherin-dependent adhesion and mechanotransduction
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The findings presented here demonstrate the role of α-catenin in cadherin-based adhesion and mechanotransduction in different mechanical contexts. Bead-twisting measurements in conjunction with imaging, and the use of different cell lines and α-catenin mutants reveal that the acute local mechanical manipulation of cadherin bonds triggers vinculin and actin recruitment to cadherin adhesions in an actin- and α-catenin-dependent manner. The modest effect of α-catenin on the two-dimensional binding affinities of cell surface cadherins further suggests that force-activated adhesion strengthening is due to enhanced cadherin–cytoskeletal interactions rather than to α-catenin-dependent affinity modulation. Complementary investigations of cadherin-based rigidity sensing also suggest that, although α-catenin alters traction force generation, it is not the sole regulator of cell contractility on compliant cadherin-coated substrata.
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Earlier in vitro work indicated vinculin as a crucial effector of cadherin-mediated mechanotransduction.
“Earlier in vitro work indicated vinculin as a crucial effector of cadherin-mediated mechanotransduction38–42.”
From E-cadherin integrates mechanotransduction and EGFR signaling to control junctional tissue polarization and tight junction positioning (2017) · cites this paper as [42]
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- Authors
- Barry, A. K., Tabdili, H., Muhamed, I., Wu, J., Shashikanth, N., Gomez, G. A., Yap, A. S., Gottardi, C. J., de Rooij, J., Wang, N., & Leckband, D. E.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- The University of Queensland (AU)
- Northwestern University (US)
- Hubrecht Institute for Developmental Biology and Stem Cell Research, University Medical Center Utrecht, 3584 CT, Utrecht, Netherlands
- Corresponding author
- Leckband, Deborah E.
- ORCID
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2014-04-15
- Volume
- 127
- Issue
- 8
- Pages
- 1779-1791
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC3986676
- OpenAlex
- W2011650280
- Cited by
- 119
- References
- 74
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 9 · 2023: 7 · 2022: 7 · 2021: 13 · 2020: 2 · 2019: 9 · 2018: 10 · 2017: 26 · 2016: 9 · 2015: 16 · 2014: 8
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Cell Science (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (5R01 GM0974, R01GM076561, R01GM097443, R01GM072744)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Keywords
- alpha-catenin, mechanotransduction, actin recruitment, rigidity sensing, cell contractility
- MeSH terms
- Actins, Animals, Binding Sites, Biomechanical Phenomena, Cell Adhesion, Dogs, Erythrocytes, Humans, Kinetics, Cadherins, Vinculin, Protein Transport, Mechanotransduction, Cellular, Cell Line, Tumor, alpha Catenin, Protein Interaction Domains and Motifs, Madin Darby Canine Kidney Cells
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