Design and evaluation of a tripartite chemogenetic fluorescent reporter for visualizing ternary protein complexes

Sara Bottone, Fanny Broch, Antoine Gedeon, Aurélien Brion, Lina El Hajji, Hela Benaissa and Arnaud Gautier ()
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Sara Bottone: Chimie Physique et Chimie du Vivant (CPCV)
Fanny Broch: Chimie Physique et Chimie du Vivant (CPCV)
Antoine Gedeon: Chimie Physique et Chimie du Vivant (CPCV)
Aurélien Brion: Chimie Physique et Chimie du Vivant (CPCV)
Lina El Hajji: Chimie Physique et Chimie du Vivant (CPCV)
Hela Benaissa: Chimie Physique et Chimie du Vivant (CPCV)
Arnaud Gautier: Chimie Physique et Chimie du Vivant (CPCV)

Nature Communications, 2025, vol. 16, issue 1, 1-14

Abstract: Abstract 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 complexes in the cytosol, at the plasma membrane, in the nucleus and at the junction of multiple organelles, opening prospects to study the role and function of multiprotein complexes in live cells and in various biologically relevant contexts.

Date: 2025
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DOI: 10.1038/s41467-025-62241-8

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