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Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1

Muscle nuclei are exposed to variable cytoplasmic strain produced by muscle contraction and relaxation, but their morphology remains stable. Still, the mechanism responsible for maintaining myonuclear architecture, and its importance, is currently elusive. Herein, we uncovered a unique myonuclear sc...

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Detalles Bibliográficos
Autores principales: Wang, Shuoshuo, Reuveny, Adriana, Volk, Talila
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4442817/
https://www.ncbi.nlm.nih.gov/pubmed/26008743
http://dx.doi.org/10.1083/jcb.201408098
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author Wang, Shuoshuo
Reuveny, Adriana
Volk, Talila
author_facet Wang, Shuoshuo
Reuveny, Adriana
Volk, Talila
author_sort Wang, Shuoshuo
collection PubMed
description Muscle nuclei are exposed to variable cytoplasmic strain produced by muscle contraction and relaxation, but their morphology remains stable. Still, the mechanism responsible for maintaining myonuclear architecture, and its importance, is currently elusive. Herein, we uncovered a unique myonuclear scaffold in Drosophila melanogaster larval muscles, exhibiting both elastic features contributed by the stretching capacity of MSP300 (nesprin) and rigidity provided by a perinuclear network of microtubules stabilized by Shot (spectraplakin) and EB1. Together, they form a flexible perinuclear shield that protects myonuclei from intrinsic or extrinsic forces. The loss of this scaffold resulted in significantly aberrant nuclear morphology and subsequently reduced levels of essential nuclear factors such as lamin A/C, lamin B, and HP1. Overall, we propose a novel mechanism for maintaining myonuclear morphology and reveal its critical link to correct levels of nuclear factors in differentiated muscle fibers. These findings may shed light on the underlying mechanism of various muscular dystrophies.
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spelling pubmed-44428172015-11-25 Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1 Wang, Shuoshuo Reuveny, Adriana Volk, Talila J Cell Biol Research Articles Muscle nuclei are exposed to variable cytoplasmic strain produced by muscle contraction and relaxation, but their morphology remains stable. Still, the mechanism responsible for maintaining myonuclear architecture, and its importance, is currently elusive. Herein, we uncovered a unique myonuclear scaffold in Drosophila melanogaster larval muscles, exhibiting both elastic features contributed by the stretching capacity of MSP300 (nesprin) and rigidity provided by a perinuclear network of microtubules stabilized by Shot (spectraplakin) and EB1. Together, they form a flexible perinuclear shield that protects myonuclei from intrinsic or extrinsic forces. The loss of this scaffold resulted in significantly aberrant nuclear morphology and subsequently reduced levels of essential nuclear factors such as lamin A/C, lamin B, and HP1. Overall, we propose a novel mechanism for maintaining myonuclear morphology and reveal its critical link to correct levels of nuclear factors in differentiated muscle fibers. These findings may shed light on the underlying mechanism of various muscular dystrophies. The Rockefeller University Press 2015-05-25 /pmc/articles/PMC4442817/ /pubmed/26008743 http://dx.doi.org/10.1083/jcb.201408098 Text en © 2015 Wang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Wang, Shuoshuo
Reuveny, Adriana
Volk, Talila
Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1
title Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1
title_full Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1
title_fullStr Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1
title_full_unstemmed Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1
title_short Nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and EB1
title_sort nesprin provides elastic properties to muscle nuclei by cooperating with spectraplakin and eb1
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4442817/
https://www.ncbi.nlm.nih.gov/pubmed/26008743
http://dx.doi.org/10.1083/jcb.201408098
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