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Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins

The generation of F-actin bundles is controlled by the action of actin-binding proteins. In Drosophila bristle development, two major actin-bundling proteins—Forked and Fascin—were identified, but still the molecular mechanism by which these actin-bundling proteins and other proteins generate bristl...

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Autores principales: Krishnan, Ramesh Kumar, Baskar, Raju, Anna, Bakhrat, Elia, Natalie, Boermel, Mandy, Bausch, Andreas R., Abdu, Uri
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8070096/
https://www.ncbi.nlm.nih.gov/pubmed/33924532
http://dx.doi.org/10.3390/ijms22084006
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author Krishnan, Ramesh Kumar
Baskar, Raju
Anna, Bakhrat
Elia, Natalie
Boermel, Mandy
Bausch, Andreas R.
Abdu, Uri
author_facet Krishnan, Ramesh Kumar
Baskar, Raju
Anna, Bakhrat
Elia, Natalie
Boermel, Mandy
Bausch, Andreas R.
Abdu, Uri
author_sort Krishnan, Ramesh Kumar
collection PubMed
description The generation of F-actin bundles is controlled by the action of actin-binding proteins. In Drosophila bristle development, two major actin-bundling proteins—Forked and Fascin—were identified, but still the molecular mechanism by which these actin-bundling proteins and other proteins generate bristle actin bundles is unknown. In this study, we developed a technique that allows recapitulation of bristle actin module organization using the Drosophila ovary by a combination of confocal microscopy, super-resolution structured illumination microscopy, and correlative light and electron microscope analysis. Since Forked generated a distinct ectopic network of actin bundles in the oocyte, the additive effect of two other actin-associated proteins, namely, Fascin and Javelin (Jv), was studied. We found that co-expression of Fascin and Forked demonstrated that the number of actin filaments within the actin bundles dramatically increased, and in their geometric organization, they resembled bristle-like actin bundles. On the other hand, co-expression of Jv with Forked increased the length and density of the actin bundles. When all three proteins co-expressed, the actin bundles were longer and denser, and contained a high number of actin filaments in the bundle. Thus, our results demonstrate that the Drosophila oocyte could serve as a test tube for actin bundle analysis.
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spelling pubmed-80700962021-04-26 Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins Krishnan, Ramesh Kumar Baskar, Raju Anna, Bakhrat Elia, Natalie Boermel, Mandy Bausch, Andreas R. Abdu, Uri Int J Mol Sci Article The generation of F-actin bundles is controlled by the action of actin-binding proteins. In Drosophila bristle development, two major actin-bundling proteins—Forked and Fascin—were identified, but still the molecular mechanism by which these actin-bundling proteins and other proteins generate bristle actin bundles is unknown. In this study, we developed a technique that allows recapitulation of bristle actin module organization using the Drosophila ovary by a combination of confocal microscopy, super-resolution structured illumination microscopy, and correlative light and electron microscope analysis. Since Forked generated a distinct ectopic network of actin bundles in the oocyte, the additive effect of two other actin-associated proteins, namely, Fascin and Javelin (Jv), was studied. We found that co-expression of Fascin and Forked demonstrated that the number of actin filaments within the actin bundles dramatically increased, and in their geometric organization, they resembled bristle-like actin bundles. On the other hand, co-expression of Jv with Forked increased the length and density of the actin bundles. When all three proteins co-expressed, the actin bundles were longer and denser, and contained a high number of actin filaments in the bundle. Thus, our results demonstrate that the Drosophila oocyte could serve as a test tube for actin bundle analysis. MDPI 2021-04-13 /pmc/articles/PMC8070096/ /pubmed/33924532 http://dx.doi.org/10.3390/ijms22084006 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Krishnan, Ramesh Kumar
Baskar, Raju
Anna, Bakhrat
Elia, Natalie
Boermel, Mandy
Bausch, Andreas R.
Abdu, Uri
Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
title Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
title_full Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
title_fullStr Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
title_full_unstemmed Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
title_short Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
title_sort recapitulating actin module organization in the drosophila oocyte reveals new roles for bristle-actin-modulating proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8070096/
https://www.ncbi.nlm.nih.gov/pubmed/33924532
http://dx.doi.org/10.3390/ijms22084006
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