ArticleMethods in molecular biology (Clifton, N.J.)2025
Using Bimolecular Fluorescence Complementation (BiFC) with Photoactivated Localization Microscopy (PALM) to Analyze Hox/Cofactor Interactions at the Super Resolution Scale in Drosophila Salivary Glands.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Bimolecular Fluorescence Complementation (BiFC) is a powerful molecular imaging method used to visualize protein-protein interactions (PPIs) in living cells or organisms. BiFC is based on the reassociation of hemi-fragments of a monomeric fluorescent protein upon spatial proximity. It is compatible with conventional light microscopy, providing a resolution that is constrained by the diffraction of light to around 250 nm. PAmCherry1, a fluorescent protein compatible for BiFC and Photoactivated Localization Microscopy (PALM), allows the analysis of PPIs with nanometer spatial resolution and single molecule sensitivity. To date, this so-called BiFC-PALM approach has only been described in human cell culture. Here, we present a protocol for performing BiFC-PALM in Drosophila larval salivary glands, using the interaction between the Hox protein Ultrabithorax (Ubx) and the generic Hox cofactor Extradenticle (Exd) as a model system.
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