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Phosphorylation Reduces the Mechanical Stability of the ?-Catenin/ ?-Catenin Complex.

ABSTRACT: The ?-catenin/?-catenin complex serves as a critical molecular interface involved in cadherin-catenin-based mechanosensing at the cell-cell adherence junction that plays a critical role in tissue integrity, repair, and embryonic development. This complex is subject to tensile forces due to internal actomyosin contractility and external mechanical micro-environmental perturbation. However, the mechanical stability of this complex has yet to be quantified. Here, we directly quantified the mechanical stability of the ?-catenin/?-catenin complex and showed that it has enough mechanical stability to survive for tens to hundreds of seconds within physiological level of forces up to 10?pN. Phosphorylation or phosphotyrosine-mimetic mutations (Y142E or/and T120E) on ?-catenin shorten the mechanical lifetime of the complex by tens of fold over the same force range. These results provide insights into the regulation of the ?-catenin/?-catenin complex by phosphorylation.

SUBMITTER: Le S

PROVIDER: S-EPMC6916283 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Phosphorylation Reduces the Mechanical Stability of the α-Catenin/ β-Catenin Complex.

Le Shimin S Yu Miao M Yan Jie J

Angewandte Chemie (International ed. in English) 20191104 51

The α-catenin/β-catenin complex serves as a critical molecular interface involved in cadherin-catenin-based mechanosensing at the cell-cell adherence junction that plays a critical role in tissue integrity, repair, and embryonic development. This complex is subject to tensile forces due to internal actomyosin contractility and external mechanical micro-environmental perturbation. However, the mechanical stability of this complex has yet to be quantified. Here, we directly quantified the mechanic ...[more]

PMID: 31625226

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