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We recently demonstrated that heteromerization of innexins 2 and 3 from  Drosophila melanogaster  ( Dm ) is crucial for epithelial organization and polarity of the embryonic epidermis. Both innexins are thought to interact via their C-terminal cytoplasmic domains during the assembly of heteromeric gap junction channels. However, the mechanisms that control heteromeric versus homomeric channel formation are still largely unknown. Here we report the isolation of both non-modified and 2′-fluoro-2′-deoxy-modified RNA anti-innexin 2 aptamers by  in vitro  selection. The aptamers bind to a proximal epitope on the carboxyl-tail of  Dm  innexin 2 protein and specifically inhibit the heterologous interaction of innexin 2 and innexin 3 carboxyl-termini  in vitro . These domain-specific inhibitors represent the first step towards functional studies focusing on the activity of these domains  in vivo .

Anti-innexin 2 aptamers specifically inhibit the heterologous interaction of the innexin 2 and innexin 3 carboxyl-termini in vitro