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Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals
Intercellular bridges are essential for fertility in many organisms. The developing fruit fly egg has become the premier model system to study intercellular bridges. During oogenesis, the oocyte is connected to supporting nurse cells by relatively large intercellular bridges, or ring canals. Once fo...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8106954/ https://www.ncbi.nlm.nih.gov/pubmed/33912915 http://dx.doi.org/10.1242/jcs.254730 |
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author | Stark, Kara Crowe, Olivia Lewellyn, Lindsay |
author_facet | Stark, Kara Crowe, Olivia Lewellyn, Lindsay |
author_sort | Stark, Kara |
collection | PubMed |
description | Intercellular bridges are essential for fertility in many organisms. The developing fruit fly egg has become the premier model system to study intercellular bridges. During oogenesis, the oocyte is connected to supporting nurse cells by relatively large intercellular bridges, or ring canals. Once formed, the ring canals undergo a 20-fold increase in diameter to support the movement of materials from the nurse cells to the oocyte. Here, we demonstrate a novel role for the conserved SH2/SH3 adaptor protein Dreadlocks (Dock) in regulating ring canal size and structural stability in the germline. Dock localizes at germline ring canals throughout oogenesis. Loss of Dock leads to a significant reduction in ring canal diameter, and overexpression of Dock causes dramatic defects in ring canal structure and nurse cell multinucleation. The SH2 domain of Dock is required for ring canal localization downstream of Src64 (also known as Src64B), and the function of one or more of the SH3 domains is necessary for the strong overexpression phenotype. Genetic interaction and localization studies suggest that Dock promotes WASp-mediated Arp2/3 activation in order to determine ring canal size and regulate growth. This article has an associated First Person interview with the first author of the paper. |
format | Online Article Text |
id | pubmed-8106954 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-81069542021-05-11 Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals Stark, Kara Crowe, Olivia Lewellyn, Lindsay J Cell Sci Research Article Intercellular bridges are essential for fertility in many organisms. The developing fruit fly egg has become the premier model system to study intercellular bridges. During oogenesis, the oocyte is connected to supporting nurse cells by relatively large intercellular bridges, or ring canals. Once formed, the ring canals undergo a 20-fold increase in diameter to support the movement of materials from the nurse cells to the oocyte. Here, we demonstrate a novel role for the conserved SH2/SH3 adaptor protein Dreadlocks (Dock) in regulating ring canal size and structural stability in the germline. Dock localizes at germline ring canals throughout oogenesis. Loss of Dock leads to a significant reduction in ring canal diameter, and overexpression of Dock causes dramatic defects in ring canal structure and nurse cell multinucleation. The SH2 domain of Dock is required for ring canal localization downstream of Src64 (also known as Src64B), and the function of one or more of the SH3 domains is necessary for the strong overexpression phenotype. Genetic interaction and localization studies suggest that Dock promotes WASp-mediated Arp2/3 activation in order to determine ring canal size and regulate growth. This article has an associated First Person interview with the first author of the paper. The Company of Biologists Ltd 2021-04-27 /pmc/articles/PMC8106954/ /pubmed/33912915 http://dx.doi.org/10.1242/jcs.254730 Text en © 2021. Published by The Company of Biologists Ltd https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Stark, Kara Crowe, Olivia Lewellyn, Lindsay Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals |
title | Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals |
title_full | Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals |
title_fullStr | Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals |
title_full_unstemmed | Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals |
title_short | Precise levels of the Drosophila adaptor protein Dreadlocks maintain the size and stability of germline ring canals |
title_sort | precise levels of the drosophila adaptor protein dreadlocks maintain the size and stability of germline ring canals |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8106954/ https://www.ncbi.nlm.nih.gov/pubmed/33912915 http://dx.doi.org/10.1242/jcs.254730 |
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