Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
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| Main Authors: | , , , |
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| Format: | Preprint |
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2024
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| _version_ | 1866911957177597952 |
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| author | Alas, Carlos D. Wu, Liying Pinaud, Fabien Haselwandter, Christoph A. |
| author_facet | Alas, Carlos D. Wu, Liying Pinaud, Fabien Haselwandter, Christoph A. |
| contents | 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 on 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. |
| format | Preprint |
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arxiv_https___arxiv_org_abs_2407_11758 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope Alas, Carlos D. Wu, Liying Pinaud, Fabien Haselwandter, Christoph A. Biological Physics Soft Condensed Matter Statistical Mechanics Adaptation and Self-Organizing Systems Subcellular Processes 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 on 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. |
| title | Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope |
| topic | Biological Physics Soft Condensed Matter Statistical Mechanics Adaptation and Self-Organizing Systems Subcellular Processes |
| url | https://arxiv.org/abs/2407.11758 |