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A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension

Integrating individual cell movements to create tissue-level shape change is essential to building an animal. We explored mechanisms of adherens junction (AJ):cytoskeleton linkage and roles of the linkage regulator Canoe/afadin during Drosophila germband extension (GBE), a convergent-extension proce...

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Autores principales: Sawyer, Jessica K., Choi, Wangsun, Jung, Kuo-Chen, He, Li, Harris, Nathan J., Peifer, Mark
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3135475/
https://www.ncbi.nlm.nih.gov/pubmed/21613546
http://dx.doi.org/10.1091/mbc.E11-05-0411
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author Sawyer, Jessica K.
Choi, Wangsun
Jung, Kuo-Chen
He, Li
Harris, Nathan J.
Peifer, Mark
author_facet Sawyer, Jessica K.
Choi, Wangsun
Jung, Kuo-Chen
He, Li
Harris, Nathan J.
Peifer, Mark
author_sort Sawyer, Jessica K.
collection PubMed
description Integrating individual cell movements to create tissue-level shape change is essential to building an animal. We explored mechanisms of adherens junction (AJ):cytoskeleton linkage and roles of the linkage regulator Canoe/afadin during Drosophila germband extension (GBE), a convergent-extension process elongating the body axis. We found surprising parallels between GBE and a quite different morphogenetic movement, mesoderm apical constriction. Germband cells have an apical actomyosin network undergoing cyclical contractions. These coincide with a novel cell shape change—cell extension along the anterior–posterior (AP) axis. In Canoe's absence, GBE is disrupted. The apical actomyosin network detaches from AJs at AP cell borders, reducing coordination of actomyosin contractility and cell shape change. Normal GBE requires planar polarization of AJs and the cytoskeleton. Canoe loss subtly enhances AJ planar polarity and dramatically increases planar polarity of the apical polarity proteins Bazooka/Par3 and atypical protein kinase C. Changes in Bazooka localization parallel retraction of the actomyosin network. Globally reducing AJ function does not mimic Canoe loss, but many effects are replicated by global actin disruption. Strong dose-sensitive genetic interactions between canoe and bazooka are consistent with them affecting a common process. We propose a model in which an actomyosin network linked at AP AJs by Canoe and coupled to apical polarity proteins regulates convergent extension.
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spelling pubmed-31354752011-09-30 A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension Sawyer, Jessica K. Choi, Wangsun Jung, Kuo-Chen He, Li Harris, Nathan J. Peifer, Mark Mol Biol Cell Articles Integrating individual cell movements to create tissue-level shape change is essential to building an animal. We explored mechanisms of adherens junction (AJ):cytoskeleton linkage and roles of the linkage regulator Canoe/afadin during Drosophila germband extension (GBE), a convergent-extension process elongating the body axis. We found surprising parallels between GBE and a quite different morphogenetic movement, mesoderm apical constriction. Germband cells have an apical actomyosin network undergoing cyclical contractions. These coincide with a novel cell shape change—cell extension along the anterior–posterior (AP) axis. In Canoe's absence, GBE is disrupted. The apical actomyosin network detaches from AJs at AP cell borders, reducing coordination of actomyosin contractility and cell shape change. Normal GBE requires planar polarization of AJs and the cytoskeleton. Canoe loss subtly enhances AJ planar polarity and dramatically increases planar polarity of the apical polarity proteins Bazooka/Par3 and atypical protein kinase C. Changes in Bazooka localization parallel retraction of the actomyosin network. Globally reducing AJ function does not mimic Canoe loss, but many effects are replicated by global actin disruption. Strong dose-sensitive genetic interactions between canoe and bazooka are consistent with them affecting a common process. We propose a model in which an actomyosin network linked at AP AJs by Canoe and coupled to apical polarity proteins regulates convergent extension. The American Society for Cell Biology 2011-07-15 /pmc/articles/PMC3135475/ /pubmed/21613546 http://dx.doi.org/10.1091/mbc.E11-05-0411 Text en © 2011 Sawyer et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Sawyer, Jessica K.
Choi, Wangsun
Jung, Kuo-Chen
He, Li
Harris, Nathan J.
Peifer, Mark
A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
title A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
title_full A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
title_fullStr A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
title_full_unstemmed A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
title_short A contractile actomyosin network linked to adherens junctions by Canoe/afadin helps drive convergent extension
title_sort contractile actomyosin network linked to adherens junctions by canoe/afadin helps drive convergent extension
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3135475/
https://www.ncbi.nlm.nih.gov/pubmed/21613546
http://dx.doi.org/10.1091/mbc.E11-05-0411
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