<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function

Nesprin-1 is a large scaffold protein connecting nuclei to the actin cytoskeleton via its KASH and Calponin Homology domains, respectively. Nesprin-1 disconnection from nuclei results in altered muscle function and myonuclei mispositioning. Furthermore, Nesprin-1 mutations are associated with muscul...

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Autores principales:	Alexandre Rey, Laurent Schaeffer, Bénédicte Durand, Véronique Morel
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Nesprin-1 Msp300 <i>Drosophila</i> myofibrils desmin isoforms Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/27bf447a258943318dbeee38c2804efc
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spelling	oai:doaj.org-article:27bf447a258943318dbeee38c2804efc2021-11-25T17:10:59Z<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function10.3390/cells101130612073-4409https://doaj.org/article/27bf447a258943318dbeee38c2804efc2021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4409/10/11/3061https://doaj.org/toc/2073-4409Nesprin-1 is a large scaffold protein connecting nuclei to the actin cytoskeleton via its KASH and Calponin Homology domains, respectively. Nesprin-1 disconnection from nuclei results in altered muscle function and myonuclei mispositioning. Furthermore, Nesprin-1 mutations are associated with muscular pathologies such as Emery Dreifuss muscular dystrophy and arthrogryposis. Nesprin-1 was thus proposed to mainly contribute to muscle function by controlling nuclei position. However, Nesprin-1′s localisation at sarcomere’s Z-discs, its involvement in organelles’ subcellular localization, as well as the description of numerous isoforms presenting different combinations of Calponin Homology (CH) and KASH domains, suggest that the contribution of Nesprin-1 to muscle functions is more complex. Here, we investigate the roles of Nesprin-1/Msp300 isoforms in muscle function and subcellular organisation using <i>Drosophila</i> larvae as a model. Subsets of Msp300 isoform were down-regulated by muscle-specific RNAi expression and muscle global function and morphology were assessed. We show that nuclei anchoring in mature muscle and global muscle function are disconnected functions associated with different Msp300 isoforms. Our work further uncovers a new and unsuspected role of Msp300 in myofibril registration and nuclei peripheral displacement supported by Msp300 CH containing isoforms, a function performed by Desmin in mammals.Alexandre ReyLaurent SchaefferBénédicte DurandVéronique MorelMDPI AGarticleNesprin-1Msp300<i>Drosophila</i>myofibrilsdesminisoformsBiology (General)QH301-705.5ENCells, Vol 10, Iss 3061, p 3061 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Nesprin-1 Msp300 <i>Drosophila</i> myofibrils desmin isoforms Biology (General) QH301-705.5
spellingShingle	Nesprin-1 Msp300 <i>Drosophila</i> myofibrils desmin isoforms Biology (General) QH301-705.5 Alexandre Rey Laurent Schaeffer Bénédicte Durand Véronique Morel <i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function
description	Nesprin-1 is a large scaffold protein connecting nuclei to the actin cytoskeleton via its KASH and Calponin Homology domains, respectively. Nesprin-1 disconnection from nuclei results in altered muscle function and myonuclei mispositioning. Furthermore, Nesprin-1 mutations are associated with muscular pathologies such as Emery Dreifuss muscular dystrophy and arthrogryposis. Nesprin-1 was thus proposed to mainly contribute to muscle function by controlling nuclei position. However, Nesprin-1′s localisation at sarcomere’s Z-discs, its involvement in organelles’ subcellular localization, as well as the description of numerous isoforms presenting different combinations of Calponin Homology (CH) and KASH domains, suggest that the contribution of Nesprin-1 to muscle functions is more complex. Here, we investigate the roles of Nesprin-1/Msp300 isoforms in muscle function and subcellular organisation using <i>Drosophila</i> larvae as a model. Subsets of Msp300 isoform were down-regulated by muscle-specific RNAi expression and muscle global function and morphology were assessed. We show that nuclei anchoring in mature muscle and global muscle function are disconnected functions associated with different Msp300 isoforms. Our work further uncovers a new and unsuspected role of Msp300 in myofibril registration and nuclei peripheral displacement supported by Msp300 CH containing isoforms, a function performed by Desmin in mammals.
format	article
author	Alexandre Rey Laurent Schaeffer Bénédicte Durand Véronique Morel
author_facet	Alexandre Rey Laurent Schaeffer Bénédicte Durand Véronique Morel
author_sort	Alexandre Rey
title	<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function
title_short	<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function
title_full	<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function
title_fullStr	<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function
title_full_unstemmed	<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function
title_sort	<i>drosophila</i> nesprin-1 isoforms differentially contribute to muscle function
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/27bf447a258943318dbeee38c2804efc
work_keys_str_mv	AT alexandrerey idrosophilainesprin1isoformsdifferentiallycontributetomusclefunction AT laurentschaeffer idrosophilainesprin1isoformsdifferentiallycontributetomusclefunction AT benedictedurand idrosophilainesprin1isoformsdifferentiallycontributetomusclefunction AT veroniquemorel idrosophilainesprin1isoformsdifferentiallycontributetomusclefunction
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<i>Drosophila</i> Nesprin-1 Isoforms Differentially Contribute to Muscle Function

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