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Background  Protein interactions control the regulatory networks underlying developmental processes. The understanding of developmental complexity will, therefore, require the characterization of protein interactions within their proper environment. The bimolecular fluorescence complementation (BiFC) technology offers this possibility as it enables the direct visualization of protein interactions in living cells. However, its potential has rarely been applied in embryos of animal model organisms and was only performed under transient protein expression levels.    Results  Using a Hox protein partnership as a test case, we investigated the suitability of BiFC for the study of protein interactions in the living  Drosophila  embryo. Importantly, all BiFC parameters were established with constructs that were stably expressed under the control of endogenous promoters. Under these physiological conditions, we showed that BiFC is specific and sensitive enough to analyse dynamic protein interactions. We next used BiFC in a candidate interaction screen, which led to the identification of several Hox protein partners.    Conclusion  Our results establish the general suitability of BiFC for revealing and studying protein interactions in their physiological context during the rapid course of  Drosophila  embryonic development.

Visualization of protein interactions in living Drosophila embryos by the bimolecular fluorescence complementation assay