Alternative molecular mechanisms for force transmission at adherens junctions via β-catenin-vinculin interaction

Nicole Morales-Camilo, Jingzhun Liu, Manuel J. Ramírez, Patricio Canales-Salgado, Juan José Alegría, Xuyao Liu, Hui Ting Ong, Nelson P. Barrera, Angélica Fierro, Yusuke Toyama, Benjamin T. Goult, Yilin Wang, Yue Meng, Ryosuke Nishimura, Kedsarin Fong-Ngern, Christine Siok Lan Low, Pakorn Kanchanawong, Jie Yan, Andrea Ravasio () and Cristina Bertocchi ()
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Nicole Morales-Camilo: Pontificia Universidad Católica De Chile
Jingzhun Liu: National University of Singapore
Manuel J. Ramírez: Pontificia Universidad Católica De Chile
Patricio Canales-Salgado: Pontificia Universidad Católica de Chile
Juan José Alegría: Pontificia Universidad Católica de Chile
Xuyao Liu: National University of Singapore
Hui Ting Ong: National University of Singapore
Nelson P. Barrera: Pontificia Universidad Católica de Chile
Angélica Fierro: Pontificia Universidad Católica de Chile
Yusuke Toyama: National University of Singapore
Benjamin T. Goult: University of Kent
Yilin Wang: National University of Singapore
Yue Meng: National University of Singapore
Ryosuke Nishimura: National University of Singapore
Kedsarin Fong-Ngern: National University of Singapore
Christine Siok Lan Low: National University of Singapore
Pakorn Kanchanawong: National University of Singapore
Jie Yan: National University of Singapore
Andrea Ravasio: Pontificia Universidad Católica de Chile
Cristina Bertocchi: Pontificia Universidad Católica De Chile

Nature Communications, 2024, vol. 15, issue 1, 1-19

Abstract: Abstract Force transmission through adherens junctions (AJs) is crucial for multicellular organization, wound healing and tissue regeneration. Recent studies shed light on the molecular mechanisms of mechanotransduction at the AJs. However, the canonical model fails to explain force transmission when essential proteins of the mechanotransduction module are mutated or missing. Here, we demonstrate that, in absence of α-catenin, β-catenin can directly and functionally interact with vinculin in its open conformation, bearing physiological forces. Furthermore, we found that β-catenin can prevent vinculin autoinhibition in the presence of α-catenin by occupying vinculin´s head-tail interaction site, thus preserving force transmission capability. Taken together, our findings suggest a multi-step force transmission process at AJs, where α-catenin and β-catenin can alternatively and cooperatively interact with vinculin. This can explain the graded responses needed to maintain tissue mechanical homeostasis and, importantly, unveils a force-bearing mechanism involving β-catenin and extended vinculin that can potentially explain the underlying process enabling collective invasion of metastatic cells lacking α-catenin.

Date: 2024
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DOI: 10.1038/s41467-024-49850-5

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