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Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium
CTP synthase (CTPS) forms a filamentous structure termed the cytoophidium in all three domains of life. The female reproductive system of Drosophila is an excellent model for studying the physiological function of cytoophidia. Here, we use CTPS(H355A), a point mutation that destroys the cytoophidium...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9740582/ https://www.ncbi.nlm.nih.gov/pubmed/36499609 http://dx.doi.org/10.3390/ijms232315282 |
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author | Wang, Qiao-Qi You, Dong-Dong Liu, Ji-Long |
author_facet | Wang, Qiao-Qi You, Dong-Dong Liu, Ji-Long |
author_sort | Wang, Qiao-Qi |
collection | PubMed |
description | CTP synthase (CTPS) forms a filamentous structure termed the cytoophidium in all three domains of life. The female reproductive system of Drosophila is an excellent model for studying the physiological function of cytoophidia. Here, we use CTPS(H355A), a point mutation that destroys the cytoophidium-forming ability of CTPS, to explore the in vivo function of cytoophidia. In CTPS(H355A) egg chambers, we observe the ingression and increased heterogeneity of follicle cells. In addition, we find that the cytoophidium-forming ability of CTPS, rather than the protein level, is the cause of the defects observed in CTPS(H355A) mutants. To sum up, our data indicate that cytoophidia play an important role in maintaining the integrity of follicle epithelium. |
format | Online Article Text |
id | pubmed-9740582 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-97405822022-12-11 Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium Wang, Qiao-Qi You, Dong-Dong Liu, Ji-Long Int J Mol Sci Article CTP synthase (CTPS) forms a filamentous structure termed the cytoophidium in all three domains of life. The female reproductive system of Drosophila is an excellent model for studying the physiological function of cytoophidia. Here, we use CTPS(H355A), a point mutation that destroys the cytoophidium-forming ability of CTPS, to explore the in vivo function of cytoophidia. In CTPS(H355A) egg chambers, we observe the ingression and increased heterogeneity of follicle cells. In addition, we find that the cytoophidium-forming ability of CTPS, rather than the protein level, is the cause of the defects observed in CTPS(H355A) mutants. To sum up, our data indicate that cytoophidia play an important role in maintaining the integrity of follicle epithelium. MDPI 2022-12-04 /pmc/articles/PMC9740582/ /pubmed/36499609 http://dx.doi.org/10.3390/ijms232315282 Text en © 2022 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 Wang, Qiao-Qi You, Dong-Dong Liu, Ji-Long Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium |
title | Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium |
title_full | Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium |
title_fullStr | Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium |
title_full_unstemmed | Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium |
title_short | Cytoophidia Maintain the Integrity of Drosophila Follicle Epithelium |
title_sort | cytoophidia maintain the integrity of drosophila follicle epithelium |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9740582/ https://www.ncbi.nlm.nih.gov/pubmed/36499609 http://dx.doi.org/10.3390/ijms232315282 |
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