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  • Letter
  • Open Access

Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope

Carlos D. Alas1,2, Liying Wu3, Fabien Pinaud1,3,4,*, and Christoph A. Haselwandter1,2,†

  • *Contact author: pinaud@usc.edu
  • †Contact author: cah77@usc.edu
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Phys. Rev. Research 7, L012019 – Published 23 January, 2025

DOI: https://doi.org/10.1103/PhysRevResearch.7.L012019

Abstract

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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Phys. Rev. Research 7, L012019– Published 23 January, 2025
  • Received 16 July 2024
  • Accepted 18 December 2024
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Published by the American Physical Society under the terms of the Creative Commons Attribution 4.0 International license. Further distribution of this work must maintain attribution to the author(s) and the published article's title, journal citation, and DOI.

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