A tripartite chemogenetic fluorescent reporter for imaging ternary protein interactions

Sara Bottone,Fanny Broch, Aurélien Brion, Lina El Hajji,Hela Benaissa,Arnaud Gautier

bioRxiv (Cold Spring Harbor Laboratory)(2023)

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Most cellular processes are carried out by multiprotein assemblies. Although various molecular tools exist to visualize binary protein interactions in live cells, the visualization of multiprotein complexes remains a challenge. Here, we report the engineering of a complementation-based approach allowing one to visualize the interaction of three proteins through effective proximity-induced complementation of three fragments of pFAST, a chemogenetic fluorescent reporter that binds and stabilizes the fluorescent state of fluorogenic chromophores (so-called fluorogens). This tripartite-split-pFAST allowed the observation of dynamic ternary protein interactions in the cytosol, at the plasma membrane and at the junction of multiple organelles, opening great prospects to study the role and function of multiprotein complexes in live cells and in various biologically relevant contexts. ### Competing Interest Statement The authors declare the following competing financial interest: A.G. is co-founder and holds equity in Twinkle Bioscience/The Twinkle Factory, a company commercializing the FAST and split-FAST technologies. The other authors declare no competing interests.
tripartite chemogenetic fluorescent reporter,ternary protein interactions,imaging
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