Apico-basal cell compression regulates Lamin A/C levels in epithelial tissues

K. Venkatesan Iyer (), Anna Taubenberger, Salma Ahmed Zeidan, Natalie A. Dye, Suzanne Eaton and Frank Jülicher ()
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K. Venkatesan Iyer: Max Planck Institute of Molecular Cell Biology and Genetics
Anna Taubenberger: Biotechnology Center TU Dresden
Salma Ahmed Zeidan: Max Planck Institute of Molecular Cell Biology and Genetics
Natalie A. Dye: Max Planck Institute of Molecular Cell Biology and Genetics
Suzanne Eaton: Max Planck Institute of Molecular Cell Biology and Genetics
Frank Jülicher: Max Planck Institute for the Physics of Complex Systems

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract The levels of nuclear protein Lamin A/C are crucial for nuclear mechanotransduction. Lamin A/C levels are known to scale with tissue stiffness and extracellular matrix levels in mesenchymal tissues. But in epithelial tissues, where cells lack a strong interaction with the extracellular matrix, it is unclear how Lamin A/C is regulated. Here, we show in epithelial tissues that Lamin A/C levels scale with apico-basal cell compression, independent of tissue stiffness. Using genetic perturbations in Drosophila epithelial tissues, we show that apico-basal cell compression regulates the levels of Lamin A/C by deforming the nucleus. Further, in mammalian epithelial cells, we show that nuclear deformation regulates Lamin A/C levels by modulating the levels of phosphorylation of Lamin A/C at Serine 22, a target for Lamin A/C degradation. Taken together, our results reveal a mechanism of Lamin A/C regulation which could provide key insights for understanding nuclear mechanotransduction in epithelial tissues.

Date: 2021
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DOI: 10.1038/s41467-021-22010-9

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