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The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos
De novo formation of cells in the Drosophila embryo is achieved when each nucleus is surrounded by a furrow of plasma membrane. Remodeling of the plasma membrane during cleavage furrow ingression involves the exocytic and endocytic pathways, including endocytic tubules that form at cleavage furrow t...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639055/ https://www.ncbi.nlm.nih.gov/pubmed/23447705 http://dx.doi.org/10.1091/mbc.E12-12-0878 |
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author | Su, Jing Chow, Brenda Boulianne, Gabrielle L. Wilde, Andrew |
author_facet | Su, Jing Chow, Brenda Boulianne, Gabrielle L. Wilde, Andrew |
author_sort | Su, Jing |
collection | PubMed |
description | De novo formation of cells in the Drosophila embryo is achieved when each nucleus is surrounded by a furrow of plasma membrane. Remodeling of the plasma membrane during cleavage furrow ingression involves the exocytic and endocytic pathways, including endocytic tubules that form at cleavage furrow tips (CFT-tubules). The tubules are marked by amphiphysin but are otherwise poorly understood. Here we identify the septin family of GTPases as new tubule markers. Septins do not decorate CFT-tubules homogeneously: instead, novel septin complexes decorate different CFT-tubules or different domains of the same CFT-tubule. Using these new tubule markers, we determine that all CFT-tubule formation requires the BAR domain of amphiphysin. In contrast, dynamin activity is preferentially required for the formation of the subset of CFT-tubules containing the septin Peanut. The absence of tubules in amphiphysin-null embryos correlates with faster cleavage furrow ingression rates. In contrast, upon inhibition of dynamin, longer tubules formed, which correlated with slower cleavage furrow ingression rates. These data suggest that regulating the recycling of membrane within the embryo is important in supporting timely furrow ingression. |
format | Online Article Text |
id | pubmed-3639055 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-36390552013-07-16 The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos Su, Jing Chow, Brenda Boulianne, Gabrielle L. Wilde, Andrew Mol Biol Cell Articles De novo formation of cells in the Drosophila embryo is achieved when each nucleus is surrounded by a furrow of plasma membrane. Remodeling of the plasma membrane during cleavage furrow ingression involves the exocytic and endocytic pathways, including endocytic tubules that form at cleavage furrow tips (CFT-tubules). The tubules are marked by amphiphysin but are otherwise poorly understood. Here we identify the septin family of GTPases as new tubule markers. Septins do not decorate CFT-tubules homogeneously: instead, novel septin complexes decorate different CFT-tubules or different domains of the same CFT-tubule. Using these new tubule markers, we determine that all CFT-tubule formation requires the BAR domain of amphiphysin. In contrast, dynamin activity is preferentially required for the formation of the subset of CFT-tubules containing the septin Peanut. The absence of tubules in amphiphysin-null embryos correlates with faster cleavage furrow ingression rates. In contrast, upon inhibition of dynamin, longer tubules formed, which correlated with slower cleavage furrow ingression rates. These data suggest that regulating the recycling of membrane within the embryo is important in supporting timely furrow ingression. The American Society for Cell Biology 2013-05-01 /pmc/articles/PMC3639055/ /pubmed/23447705 http://dx.doi.org/10.1091/mbc.E12-12-0878 Text en © 2013 Su 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 BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Su, Jing Chow, Brenda Boulianne, Gabrielle L. Wilde, Andrew The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos |
title | The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos |
title_full | The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos |
title_fullStr | The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos |
title_full_unstemmed | The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos |
title_short | The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in Drosophila embryos |
title_sort | bar domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization in drosophila embryos |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639055/ https://www.ncbi.nlm.nih.gov/pubmed/23447705 http://dx.doi.org/10.1091/mbc.E12-12-0878 |
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