Evidence map›Paper›PMID 28406179›Full record

ArticleScientific reports2017

Genetic visualization of protein interactions harnessing liquid phase transitions.

Taku Watanabe, Tatsuya Seki, Takashi Fukano, Asako Sakaue-Sawano, Satoshi Karasawa, Misaki Kubota, Hiroshi Kurokawa, Ken Inoue, Junichi Akatsuka, Atsushi Miyawaki

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
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  4. Chemical reviews · 2026
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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

10 authors.

Taku WatanabeLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Tatsuya SekiLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Takashi FukanoLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Asako Sakaue-SawanoLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Satoshi KarasawaLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Misaki KubotaLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Hiroshi KurokawaLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.
Ken InoueIna Laboratory, Medical &Biological Laboratories Co., Ltd., Ina, Nagano, Japan.
Junichi AkatsukaIna Laboratory, Medical &Biological Laboratories Co., Ltd., Ina, Nagano, Japan.
Atsushi MiyawakiLaboratory for Cell Function and Dynamics, Brain Science Institute, RIKEN, Saitama 351-0198, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions (PPIs) are essential components of cellular function. Current fluorescence-based technologies to measure PPIs have limited dynamic range and quantitative reproducibility. Here, we describe a genetically-encoded PPI visualization system that harnesses the dynamics of condensed liquid-phase transitions to analyze protein interactions in living cells. The fluorescent protein Azami-Green and p62-PB1 domain when fused to PPI partners triggered a rapid concatenation/oligomerization process that drove the condensation of liquid-phase droplets for real-time analysis of the interaction with unlimited dynamic range in the fluorescence signal. Proof-of-principle studies revealed novel insights on the live cell dynamics of XIAP-Smac and ERK2-dimer interactions. A photoconvertible variant allowed time-resolved optical highlighting for PPI kinetic analysis. Our system, called Fluoppi, demonstrates the unique signal amplification properties of liquid-phase condensation to detect PPIs. The findings introduce a general method for discovery of novel PPIs and modulators of established PPIs.

Indexed as

Apoptosis Regulatory ProteinsBinding SitesBiophysical PhenomenaFluorescent DyesHeLa CellsHumansIntracellular Signaling Peptides and ProteinsKineticsMitochondrial ProteinsMitogen-Activated Protein Kinase 1Protein DomainsProtein Interaction MappingProteinsRNA-Binding ProteinsX-Linked Inhibitor of Apoptosis ProteinApoptosis Regulatory ProteinsDIABLO protein, humanFluorescent DyesIntracellular Signaling Peptides and ProteinsMAPK1 protein, humanMitochondrial ProteinsMitogen-Activated Protein Kinase 1P62 protein, humanProteinsRNA-Binding ProteinsXIAP protein, humanX-Linked Inhibitor of Apoptosis Protein

Identifiers

PMID28406179
PMCPMC5390312

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Registered trials

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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 OpenQuestion graph.