Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis

Contractile actomyosin networks generate forces that drive tissue morphogenesis. Actomyosin contractility is controlled primarily by reversible phosphorylation of the myosin-II regulatory light chain through the action of myosin kinases and phosphatases. While the role of myosin light-chain kinase i...

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Autores: Valencia-Expósito, Andrea, Grosheva, Inna, Míguez, David G., González-Reyes, Acaimo, Martín-Bermudo, María D.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2016
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/163361
Acceso en línea:http://hdl.handle.net/10261/163361
Access Level:acceso abierto
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spelling Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesisValencia-Expósito, AndreaGrosheva, InnaMíguez, David G.González-Reyes, AcaimoMartín-Bermudo, María D.Contractile actomyosin networks generate forces that drive tissue morphogenesis. Actomyosin contractility is controlled primarily by reversible phosphorylation of the myosin-II regulatory light chain through the action of myosin kinases and phosphatases. While the role of myosin light-chain kinase in regulating contractility during morphogenesis has been largely characterized, there is surprisingly little information on myosin light-chain phosphatase (MLCP) function in this context. Here, we use live imaging of Drosophila follicle cells combined with mathematical modelling to demonstrate that the MLCP subunit flapwing (flw) is a key regulator of basal myosin oscillations and cell contractions underlying egg chamber elongation. Flw expression decreases specifically on the basal side of follicle cells at the onset of contraction and flw controls the initiation and periodicity of basal actomyosin oscillations. Contrary to previous reports, basal F-actin pulsates similarly to myosin. Finally, we propose a quantitative model in which periodic basal actomyosin oscillations arise in a cell-autonomous fashion from intrinsic properties of motor assemblies.Research in our laboratories is funded by the Spanish Ministerio de Economía y Competitividad and the FEDER programme (BFU2013-48988-C2-1-P to M.D.M.-B, BFU2012-35446 to A.G.-R., BFU2011-30303 and BFU2010-18959 to D.G.M.) and by the Junta de Andalucía (Proyecto de Excelencia P09-CVI-5058). I.G. was supported by a JAE-DOC (CSIC) and D.G.M. by a Ramon y Cajal Fellowship (Ministerio Español de Economía y Competitividad Ref. RYC-2010-07450) and a Marie Curie International Reintegration Grant (EU, Ref. 248346-NMSSBLS).Peer ReviewedNature Publishing GroupConsejo Superior de Investigaciones Científicas (España)Junta de AndalucíaEuropean CommissionMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2018201820162018info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/163361reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/EC/FP7/248346info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-48988-C2-1-Phttps://doi.org/10.1038/ncomms10746Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1633612026-05-22T06:33:51Z
dc.title.none.fl_str_mv Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
title Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
spellingShingle Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
Valencia-Expósito, Andrea
title_short Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
title_full Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
title_fullStr Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
title_full_unstemmed Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
title_sort Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
dc.creator.none.fl_str_mv Valencia-Expósito, Andrea
Grosheva, Inna
Míguez, David G.
González-Reyes, Acaimo
Martín-Bermudo, María D.
author Valencia-Expósito, Andrea
author_facet Valencia-Expósito, Andrea
Grosheva, Inna
Míguez, David G.
González-Reyes, Acaimo
Martín-Bermudo, María D.
author_role author
author2 Grosheva, Inna
Míguez, David G.
González-Reyes, Acaimo
Martín-Bermudo, María D.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas (España)
Junta de Andalucía
European Commission
Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description Contractile actomyosin networks generate forces that drive tissue morphogenesis. Actomyosin contractility is controlled primarily by reversible phosphorylation of the myosin-II regulatory light chain through the action of myosin kinases and phosphatases. While the role of myosin light-chain kinase in regulating contractility during morphogenesis has been largely characterized, there is surprisingly little information on myosin light-chain phosphatase (MLCP) function in this context. Here, we use live imaging of Drosophila follicle cells combined with mathematical modelling to demonstrate that the MLCP subunit flapwing (flw) is a key regulator of basal myosin oscillations and cell contractions underlying egg chamber elongation. Flw expression decreases specifically on the basal side of follicle cells at the onset of contraction and flw controls the initiation and periodicity of basal actomyosin oscillations. Contrary to previous reports, basal F-actin pulsates similarly to myosin. Finally, we propose a quantitative model in which periodic basal actomyosin oscillations arise in a cell-autonomous fashion from intrinsic properties of motor assemblies.
publishDate 2016
dc.date.none.fl_str_mv 2016
2018
2018
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/163361
url http://hdl.handle.net/10261/163361
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
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#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/EC/FP7/248346
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2013-48988-C2-1-P
https://doi.org/10.1038/ncomms10746

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
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