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Transcriptomes of somatic and germ line cells in the developing larval ovary of Drosophila melanogaster in wild type, hpoRNAi and ykiRNAi conditions.

ABSTRACT: Adult insect ovaries are made up of egg production structures called ovarioles, whose number is directly linked to fecundity and fitness. Ovariole number is directly determined by the number of cell stacks called terminal filaments in the larval ovary, which in turn is determined by the number of terminal filament cells available to form terminal filaments. Elucidating the developmental and genetic regulation of terminal filament cell proliferation is thus key to understanding the regulation of adult ovariole number and fitness. Our previous work showed that the Hippo signaling pathway, including the kinase hippo and the transcription factor yorkie, regulate terminal filament cell number in Drosophila melanogaster. To identify the specific transcriptional responses of ovarian cells to Hippo signaling during ovary development, we systematically measured mRNA expression in isolated pools of somatic and germ line cells from the Drosophila larval ovary at the beginning, middle and end of terminal filament formation using RNA-seq. We performed these RNA-seq experiments in wild type, hippoRNAi and yorkieRNAi genetic backgrounds at each of these three developmental stages.

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE250320 | GEO | 2025/07/29

REPOSITORIES: GEO

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Project description:Neurodegenerative diseases are characterised by the abnormal filamentous assembly of specific proteins in the central nervous system1. Human genetic studies established a causal role for protein assembly in neurodegeneration2. However, the underlying molecular mechanisms remain largely unknown, which is limiting progress in developing clinical tools for these diseases. Recent advances in electron cryo- microscopy (cryo-EM) have enabled the structures of the protein filaments to be determined from patient brains1. All diseases studied to date have been characterised by the self-assembly of proteins in homomeric amyloid filaments, including that of TAR DNA-binding protein 43 (TDP-43) in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) Types A and B3,4. Here, we used cryo-EM to determine filament structures from the brains of individuals with FTLD-TDP Type C, one of the most common forms of sporadic FTLD- TDP. Unexpectedly, the structures revealed that a second protein, annexin A11 (ANXA11), co-assembles with TDP-43 in heteromeric amyloid filaments. The ordered filament fold is formed by TDP-43 residues G282/284–N345 and ANXA11 residues L39– Y74 from their respective low-complexity domains (LCDs). Regions of TDP-43 and ANXA11 previously implicated in protein-protein interactions form an extensive hydrophobic interface at the centre of the filament fold. Immunoblots of the filaments revealed that the majority of ANXA11 exists as a ~22 kDa N-terminal fragment (NTF) lacking the annexin core domain. Immunohistochemistry of brain sections showed the co-localisation of ANXA11 and TDP-43 in inclusions, redefining the histopathology of FTLD-TDP Type C. This work establishes a central role for ANXA11 in FTLD-TDP Type C. The unprecedented formation of heteromeric amyloid filaments in human brain revises our understanding of amyloid assembly and may be of significance for the pathogenesis of neurodegenerative diseases.

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Transcriptomes of somatic and germ line cells in the developing larval ovary of Drosophila melanogaster in wild type, hpoRNAi and ykiRNAi conditions.

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