Evidence map›Paper›PMID 40730719›Full record

ArticleNature communications2025

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, Arnaud Gautier

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Protein Engineering for Spatiotemporally Resolved Cellular Monitoring.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Sara Bottone *Sorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France.ORCID http://orcid.org/0000-0002-4049-2332
Fanny Broch *Sorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France.
Antoine GedeonSorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France.ORCID http://orcid.org/0000-0003-0301-8786
Aurélien BrionSorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France.
Lina El HajjiSorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France.
Hela BenaissaSorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France.
Arnaud GautierSorbonne Université, École Normale Supérieure, Université PSL, CNRS, Chimie Physique et Chimie du Vivant (CPCV), Paris, France. arnaud.gautier@sorbonne-universite.fr.ORCID http://orcid.org/0000-0003-1017-9879

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) ERC-2016-CoG-724705
6 · The paper itself

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.

Indexed as

Fluorescent DyesMultiprotein ComplexesCell MembraneCell NucleusChemogeneticsCytosolGenes, ReporterHEK293 CellsHeLa CellsHumansMicroscopy, FluorescenceFluorescent DyesMultiprotein Complexes

Identifiers

PMID40730719
PMCPMC12307597

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.