ArticleScientific reports2018
The indispensable contribution of s38 protein to ovarian-eggshell morphogenesis in Drosophila melanogaster.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Review
- Amyloid Fibrils of the s36 Protein Modulate the Morphogenesis ofInternational journal of molecular sciences · 2024Article
- Comparative Transcriptomic Analysis Revealing the Potential Mechanisms of Erythritol-Caused Mortality and Oviposition Inhibition inInternational journal of molecular sciences · 2024Article
- Finishing the egg.Genetics · 2024Article
- Knockdown of Sec16 causes early lethality and defective deposition of the protein Rp30 in the eggshell of the vectorFrontiers in cell and developmental biology · 2024Article
- Nanoscale Prognosis of Colorectal Cancer Metastasis from AFM Image Processing of Histological Sections.Cancers · 2023Article
- Vitelline Membrane Protein 26 Mutagenesis, Using CRISPR/Cas9, Results in Egg Collapse inInternational journal of molecular sciences · 2022Article
- ATG3 Is Important for the Chorion Ultrastructure During Oogenesis in the Insect VectorFrontiers in physiology · 2021Article
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Authors and funding
15 authors.
Funding
Abstract
Drosophila chorion represents a remarkable model system for the in vivo study of complex extracellular-matrix architectures. For its organization and structure, s38 protein is considered as a component of major importance, since it is synthesized and secreted during early choriogenesis. However, there is no evidence that proves its essential, or redundant, role in chorion biogenesis. Hence, we show that targeted downregulation of s38 protein, specifically in the ovarian follicle-cell compartment, via employment of an RNAi-mediated strategy, causes generation of diverse dysmorphic phenotypes, regarding eggshell's regionally and radially specialized structures. Downregulation of s38 protein severely impairs fly's fertility and is unable to be compensated by the s36 homologous family member, thus unveiling s38 protein's essential contribution to chorion's assembly and function. Altogether, s38 acts as a key skeletal protein being critically implicated in the patterning establishment of a highly structured tripartite endochorion. Furthermore, it seems that s38 loss may sensitize choriogenesis to stochastic variation in its coordination and timing.
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