Related Experiment Video
Updated: Dec 17, 2025

Integration of Bioinformatics Approaches and Experimental Validations to Understand the Role of Notch Signaling in Ovarian Cancer
Published on: January 12, 2020
BmCAP, a silkmoth gene encoding multiple protein isoforms characterized by SoHo and SH3 domains: expression analysis
Theodoros Georgomanolis1, Kostas Iatrou, Luc Swevers
1Insect Molecular Genetics and Biotechnology, Institute of Biology, National Centre for Scientific Research Demokritos, Aghia Paraskevi Attikis, Athens, Greece.
Abstract:
CAP/ArgBP2/vinexin family proteins, adaptor proteins characterized by three SH3 domains at their C-termini and a SoHo domain towards their N-termini, are known to regulate cell adhesion, cytoskeletal organization, and growth factor signaling. Here we present the isolation and ovarian expression of the BmCAP gene which encodes CAP/ArgBP2/vinexin family proteins in the silkmoth, Bombyx mori. Screening for full-length cDNA clones identified three mRNA isoforms, BmCAP-A1, BmCAP-A2 and BmCAP-B, which show expression throughout ovarian follicular development. Using an antibody raised against a unique region between the SoHo and SH3 domains, BmCAP-A protein isoforms were identified that show specific expression in different compartments of the ovarian follicles. Immunofluorescence staining of the cells of the follicular epithelium establishes a dynamic pattern of BmCAP-A protein localization during choriogenesis. During early choriogenesis, BmCAP-A has a diffuse localization in the cytoplasm but could also be found concentrated at the apical and basal sides at the cell-cell junctions. During late choriogenesis, the diffuse cytoplasmic staining of BmCAP-A disappears while the staining pattern at the apical side resembles a blueprint for the eggshell surface structure. We suggest that BmCAP-A isoforms have important functions during ovarian development, which involve not only the traditional roles in actin organization or cell-cell adhesion but also the regulation of secretion of chorion proteins and the sculpting of the chorion surface.

