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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...

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Detalles Bibliográficos
Autores principales: Stark, Kara, Crowe, Olivia, Lewellyn, Lindsay
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2021
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.
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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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