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Apico-basal cell compression regulates Lamin A/C levels in epithelial tissues
K Venkatesan Iyer1,2,3, Anna Taubenberger4, Salma Ahmed Zeidan5
1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany. iyer@mpi-cbg.de.
Nature Communications
|March 26, 2021
Summary
Nuclear Lamin A/C levels in epithelial tissues are regulated by cell compression, not stiffness. Cell compression deforms nuclei, impacting Lamin A/C phosphorylation and degradation, revealing a novel mechanotransduction pathway.
Area of Science:
- Cell Biology
- Biophysics
- Mechanobiology
Background:
- Nuclear Lamin A/C is vital for nuclear mechanotransduction.
- Lamin A/C levels correlate with tissue stiffness in mesenchymal tissues.
- Regulation of Lamin A/C in epithelial tissues, which have limited extracellular matrix interaction, remains unclear.
Purpose of the Study:
- To investigate the regulation of Lamin A/C levels in epithelial tissues.
- To determine the relationship between cell compression, nuclear deformation, and Lamin A/C levels.
- To elucidate the molecular mechanisms underlying Lamin A/C regulation in epithelial cells.
Main Methods:
- Genetic perturbations in Drosophila epithelial tissues.
- Analysis of Lamin A/C levels in response to apico-basal cell compression.
- Investigation of nuclear deformation and Lamin A/C phosphorylation at Serine 22 in mammalian epithelial cells.
Main Results:
- Lamin A/C levels in epithelial tissues scale with apico-basal cell compression, irrespective of tissue stiffness.
- Apico-basal cell compression induces nuclear deformation, regulating Lamin A/C levels.
- Nuclear deformation modulates Lamin A/C phosphorylation at Serine 22, a key site for degradation.
Conclusions:
- Cellular compression, not tissue stiffness, is a primary regulator of Lamin A/C in epithelial tissues.
- Nuclear deformation acts as a mechanical signal to control Lamin A/C levels via phosphorylation.
- This study uncovers a novel mechanism for nuclear mechanotransduction in epithelial cells.
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