Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
Emerin, a nuclear membrane protein with important biological roles in mechanotransduction and nuclear shape adaptation, self-assembles into nanometer-size domains at the inner nuclear membrane. The size and emerin occupancy of these nanodomains change with applied mechanical stress as well as under...
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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
American Physical Society
2025-01-01
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| Series: | Physical Review Research |
| Online Access: | http://doi.org/10.1103/PhysRevResearch.7.L012019 |
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| Summary: | Emerin, a nuclear membrane protein with important biological roles in mechanotransduction and nuclear shape adaptation, self-assembles into nanometer-size domains at the inner nuclear membrane. The size and emerin occupancy of these nanodomains change with applied mechanical stress as well as under emerin mutations associated with Emery-Dreifuss muscular dystrophy (EDMD). Through a combination of theory and experiment, we show here that a simple reaction-diffusion model explains the self-assembly of emerin nanodomains. Our model yields quantitative agreement with experimental observations on the size and occupancy of emerin nanodomains for wild-type emerin and EDMD-associated mutations of emerin, with and without applied forces, and allows successful prediction of emerin diffusion coefficients from observations of the overall properties of emerin nanodomains. Our results provide a physical understanding of EDMD-associated defects in emerin organization in terms of changes in key reaction and diffusion properties of emerin and its nuclear binding partners. |
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| ISSN: | 2643-1564 |