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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
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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. |
format | Online Article Text |
id | pubmed-3135475 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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