Abstract
Visualization of protein–protein interactions in vivo offers a powerful tool to resolve spatial and temporal aspects of cellular functions. The bimolecular fluorescence complementation (BiFC) makes use of nonfluorescent fragments of green fluorescent protein or its variants that are added as “tags” to target proteins under study. Only upon target protein interaction is a fluorescent protein complex assembled, and the site of interaction can be monitored by microscopy. In this chapter, we describe the method and tools for the use of BiFC in the yeast Saccharomyces cerevisiae and in mammalian cells.
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Acknowledgments
Chang-Deng Hu is acknowledged for EYFP fragment-containing plasmids and comments on the manuscript. The work was supported by the Academy of Finland grant No. 257409 to M.W.-B. and 133552 to J.J., the Sigrid Juselius Foundation, the Liv och Hälsa Foundation, the Novo Nordisk Foundation, the Magnus Ehrnrooth Foundation (to V.M.O.), and the National Basic Research Program of China (2012CB517502 to D.Y.)
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Weber-Boyvat, M., Li, S., Skarp, KP., Olkkonen, V.M., Yan, D., Jäntti, J. (2015). Bimolecular Fluorescence Complementation (BiFC) Technique in Yeast Saccharomyces cerevisiae and Mammalian Cells. In: Tang, B. (eds) Membrane Trafficking. Methods in Molecular Biology, vol 1270. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2309-0_20
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DOI: https://doi.org/10.1007/978-1-4939-2309-0_20
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