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: Carlos D. Alas, Liying Wu, Fabien Pinaud, Christoph A. Haselwandter
Format: Article
Language:English
Published: American Physical Society 2025-01-01
Series:Physical Review Research
Online Access:http://doi.org/10.1103/PhysRevResearch.7.L012019
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author Carlos D. Alas
Liying Wu
Fabien Pinaud
Christoph A. Haselwandter
author_facet Carlos D. Alas
Liying Wu
Fabien Pinaud
Christoph A. Haselwandter
author_sort Carlos D. Alas
collection DOAJ
description 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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publisher American Physical Society
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spelling doaj-art-6504663883da4deeb5d8247fdc32583c2025-01-23T15:01:19ZengAmerican Physical SocietyPhysical Review Research2643-15642025-01-0171L01201910.1103/PhysRevResearch.7.L012019Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelopeCarlos D. AlasLiying WuFabien PinaudChristoph A. HaselwandterEmerin, 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.http://doi.org/10.1103/PhysRevResearch.7.L012019
spellingShingle Carlos D. Alas
Liying Wu
Fabien Pinaud
Christoph A. Haselwandter
Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
Physical Review Research
title Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
title_full Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
title_fullStr Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
title_full_unstemmed Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
title_short Diffusion-driven self-assembly of emerin nanodomains at the nuclear envelope
title_sort diffusion driven self assembly of emerin nanodomains at the nuclear envelope
url http://doi.org/10.1103/PhysRevResearch.7.L012019
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AT liyingwu diffusiondrivenselfassemblyofemerinnanodomainsatthenuclearenvelope
AT fabienpinaud diffusiondrivenselfassemblyofemerinnanodomainsatthenuclearenvelope
AT christophahaselwandter diffusiondrivenselfassemblyofemerinnanodomainsatthenuclearenvelope