A feedback circuitry involving γ-actin, β-actin and nonmuscle myosin-2 A controls tight junction and apical cortex mechanics

Marine Maupérin, Yuze Sun, Thomas Glandorf, Tabea Anne Oswald, Niklas Klatt, Burkhard Geil, Annick Mutero-Maeda, Isabelle Méan, Lionel Jond, Andreas Janshoff, Jie Yan and Sandra Citi ()
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Marine Maupérin: University of Geneva
Yuze Sun: National University of Singapore
Thomas Glandorf: Institute for Physical Chemistry
Tabea Anne Oswald: Institute for Organic and Biomolecular Chemistry
Niklas Klatt: Institute for Physical Chemistry
Burkhard Geil: Institute for Physical Chemistry
Annick Mutero-Maeda: University of Geneva
Isabelle Méan: University of Geneva
Lionel Jond: University of Geneva
Andreas Janshoff: Institute for Physical Chemistry
Jie Yan: National University of Singapore
Sandra Citi: University of Geneva

Nature Communications, 2025, vol. 16, issue 1, 1-14

Abstract: Abstract Cytoplasmic β- and γ-actin isoforms, along with non-muscle myosin 2 isoforms, are tightly regulated in epithelial cells and compose the actomyosin cytoskeleton at the apical junctional complex. However, their specific role in regulating the mechanics of the membrane cortex and the organization of junctions, and which biomechanical circuitries modulate their expression remain poorly understood. Here, we show that γ-actin depletion in MDCK and other epithelial cells results in increased expression and junctional accumulation of β-actin and increased tight junction membrane tortuosity, both dependent on nonmuscle myosin-2A upregulation. The knock-out of γ-actin also decreases apical membrane stiffness and increases dynamic exchange of the cytoplasmic tight junction proteins like ZO-1 and cingulin, without affecting tight junction organization and barrier function. In summary, our findings uncover a biomechanical circuitry linking γ-actin to β-actin expression through nonmuscle myosin-2A and reveal γ-actin as a key regulator of tight junction and apical membrane cortex mechanics, and the dynamics of cytoskeleton-associated tight junction proteins in epithelial cells.

Date: 2025
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DOI: 10.1038/s41467-025-57428-y

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