Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.

<h4>Background</h4>The myosin phosphatase is a highly conserved regulator of actomyosin contractility. Zebrafish has emerged as an ideal model system to study the in vivo role of myosin phosphatase in controlling cell contractility, cell movement and epithelial biology. Most work in zebr...

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Autores principales:	Vaishali Jayashankar, Michael J Nguyen, Brandon W Carr, Dale C Zheng, Joseph B Rosales, Joshua B Rosales, Douglas C Weiser
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/923b3f0e633242148174a41e1dd00759
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spelling	oai:doaj.org-article:923b3f0e633242148174a41e1dd007592021-11-18T08:55:39ZProtein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.1932-620310.1371/journal.pone.0075766https://doaj.org/article/923b3f0e633242148174a41e1dd007592013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24040418/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>The myosin phosphatase is a highly conserved regulator of actomyosin contractility. Zebrafish has emerged as an ideal model system to study the in vivo role of myosin phosphatase in controlling cell contractility, cell movement and epithelial biology. Most work in zebrafish has focused on the regulatory subunit of the myosin phosphatase called Mypt1. In this work, we examined the critical role of Protein Phosphatase 1, PP1, the catalytic subunit of the myosin phosphatase.<h4>Methodology/principal findings</h4>We observed that in zebrafish two paralogous genes encoding PP1β, called ppp1cba and ppp1cbb, are both broadly expressed during early development. Furthermore, we found that both gene products interact with Mypt1 and assemble an active myosin phosphatase complex. In addition, expression of this complex results in dephosphorylation of the myosin regulatory light chain and large scale rearrangements of the actin cytoskeleton. Morpholino knock-down of ppp1cba and ppp1cbb results in severe defects in morphogenetic cell movements during gastrulation through loss of myosin phosphatase function.<h4>Conclusions/significance</h4>Our work demonstrates that zebrafish have two genes encoding PP1β, both of which can interact with Mypt1 and assemble an active myosin phosphatase. In addition, both genes are required for convergence and extension during gastrulation and correct dosage of the protein products is required.Vaishali JayashankarMichael J NguyenBrandon W CarrDale C ZhengJoseph B RosalesJoshua B RosalesDouglas C WeiserPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e75766 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Vaishali Jayashankar Michael J Nguyen Brandon W Carr Dale C Zheng Joseph B Rosales Joshua B Rosales Douglas C Weiser Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
description	<h4>Background</h4>The myosin phosphatase is a highly conserved regulator of actomyosin contractility. Zebrafish has emerged as an ideal model system to study the in vivo role of myosin phosphatase in controlling cell contractility, cell movement and epithelial biology. Most work in zebrafish has focused on the regulatory subunit of the myosin phosphatase called Mypt1. In this work, we examined the critical role of Protein Phosphatase 1, PP1, the catalytic subunit of the myosin phosphatase.<h4>Methodology/principal findings</h4>We observed that in zebrafish two paralogous genes encoding PP1β, called ppp1cba and ppp1cbb, are both broadly expressed during early development. Furthermore, we found that both gene products interact with Mypt1 and assemble an active myosin phosphatase complex. In addition, expression of this complex results in dephosphorylation of the myosin regulatory light chain and large scale rearrangements of the actin cytoskeleton. Morpholino knock-down of ppp1cba and ppp1cbb results in severe defects in morphogenetic cell movements during gastrulation through loss of myosin phosphatase function.<h4>Conclusions/significance</h4>Our work demonstrates that zebrafish have two genes encoding PP1β, both of which can interact with Mypt1 and assemble an active myosin phosphatase. In addition, both genes are required for convergence and extension during gastrulation and correct dosage of the protein products is required.
format	article
author	Vaishali Jayashankar Michael J Nguyen Brandon W Carr Dale C Zheng Joseph B Rosales Joshua B Rosales Douglas C Weiser
author_facet	Vaishali Jayashankar Michael J Nguyen Brandon W Carr Dale C Zheng Joseph B Rosales Joshua B Rosales Douglas C Weiser
author_sort	Vaishali Jayashankar
title	Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
title_short	Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
title_full	Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
title_fullStr	Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
title_full_unstemmed	Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
title_sort	protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/923b3f0e633242148174a41e1dd00759
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Protein phosphatase 1 β paralogs encode the zebrafish myosin phosphatase catalytic subunit.

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