The indispensable contribution of s38 protein to ovarian-eggshell morphogenesis in Drosophila melanogaster

Autor:	Issidora S. Papassideri, Athanasios Anagnostopoulos, Stamatia A. Katarachia, Dimitrios J. Stravopodis, A.C. Cefalas, George Th. Tsangaris, Niki E. Sagioglou, Panagiotis D. Velentzas, Maria M. Tsioka, Vassilios Gavriil, Eleni V. Thanou, Evangelia Sarantopoulou, Zoe Kollia, Athanassios D. Velentzas, Vassiliki E. Mpakou
Rok vydání:	2018
Předmět:	0301 basic medicine Science Morphogenesis Down-Regulation Article 03 medical and health sciences Egg Shell 0302 clinical medicine Downregulation and upregulation Ovarian Follicle Chorion Proteins Compartment (development) Animals Drosophila Proteins Endochorion Choriogenesis Lays Eggs Ovum Multidisciplinary biology Adhesion Force Values Egg Proteins Chorion Dorsal Appendages biology.organism_classification Phenotype Cell biology Cell Compartmentation 030104 developmental biology Drosophila melanogaster Fertility Gene Expression Regulation Medicine Female RNA Interference 030217 neurology & neurosurgery Function (biology) Biogenesis
Zdroj:	Scientific Reports Scientific Reports, Vol 8, Iss 1, Pp 1-17 (2018)
ISSN:	2045-2322
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fca9273f2da036fe18e9b4f36b751093 https://pubmed.ncbi.nlm.nih.gov/30382186 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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