Bimolecular fluorescence complementation (BiFC) analysis of protein-protein interactions and assessment of subcellular localization in live cells

17Citations
Citations of this article
23Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Bimolecular fluorescence complementation (BiFC) is a fluorescence imaging technique used to visualize protein-protein interactions (PPIs) in live cells and animals. One unique application of BiFC is to reveal subcellular localization of PPIs. The superior signal-to-noise ratio of BiFC in comparison with fluorescence resonance energy transfer or bioluminescence resonance energy transfer enables its wide applications. Here, we describe how confocal microscopy can be used to detect and quantify PPIs and their subcellular localization. We use basic leucine zipper transcription factor proteins as an example to provide a step-by- step BiFC protocol using a Nikon A1 confocal microscope and NIS-Elements imaging software. The protocol given below can be readily adapted for use with other confocal microscopes or imaging software.

Cite

CITATION STYLE

APA

Pratt, E. P. S., Owens, J. L., Hockerman, G. H., & Hu, C. D. (2016). Bimolecular fluorescence complementation (BiFC) analysis of protein-protein interactions and assessment of subcellular localization in live cells. In Methods in Molecular Biology (Vol. 1474, pp. 153–170). Humana Press Inc. https://doi.org/10.1007/978-1-4939-6352-2_9

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free