Evidence map›Paper›PMID 34588591›Full record

ArticleScientific reports2021

Molecular principles of recruitment and dynamics of guest proteins in liquid droplets.

Kiyoto Kamagata, Nanako Iwaki, Milan Kumar Hazra, Saori Kanbayashi, Trishit Banerjee, Rika Chiba, Seiji Sakomoto, Virginie Gaudon, Bertrand Castaing, Hiroto Takahashi and 4 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  6. Evolutionarily conserved grammar rules viral factories of amoeba-infecting members of the hyperdiverseProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Lipid-induced condensate formation from the Alzheimer's Aβ peptide triggers amyloid aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  14. Article
  15. Protein conformation and biomolecular condensates.Current research in structural biology · 2022
    Review
  16. 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

14 authors at 5 institutions in 3 countries.

Kiyoto Kamagata *Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan. kiyoto.kamagata.e8@tohoku.ac.jp.
Nanako Iwaki *Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Milan Kumar HazraDepartment of Structural Biology, Weizmann Institute of Science, 76100, Rehovot, Israel.
Saori KanbayashiInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Trishit BanerjeeInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Rika ChibaInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Seiji SakomotoDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Virginie GaudonCentre de Biophysique Moléculaire, CNRS, UPR4301, rue Charles Sadron, 45072, Orléans, France.
Bertrand CastaingCentre de Biophysique Moléculaire, CNRS, UPR4301, rue Charles Sadron, 45072, Orléans, France.
Hiroto TakahashiInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Michiko KimuraInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Hiroyuki OikawaInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Satoshi TakahashiInstitute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, 980-8577, Japan.
Yaakov LevyDepartment of Structural Biology, Weizmann Institute of Science, 76100, Rehovot, Israel.
Tohoku University · JPWeizmann Institute of Science · ILCentre de Biophysique Moléculaire · FRCentre National de la Recherche Scientifique · FRKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the continuous discovery of host and guest proteins in membraneless organelles, complex host-guest interactions hinder the understanding of the molecular grammar governing liquid-liquid phase separation. In this study, we characterized the localization and dynamic properties of guest proteins in liquid droplets using single-molecule fluorescence microscopy. Eighteen guest proteins of different sizes, structures, and oligomeric states were examined in host p53 liquid droplets. Recruitment did not significantly depend on the structural properties of the guest proteins, but was moderately correlated with their length, total charge, and number of R and Y residues. In contrast, the diffusion of disordered guest proteins was comparable to that of host p53, whereas that of folded proteins varied widely. Molecular dynamics simulations suggest that folded proteins diffuse within the voids of the liquid droplet while interacting weakly with neighboring host proteins, whereas disordered proteins adapt their structures to form tight interactions with the host proteins. Our study provides insights into the key molecular principles of the localization and dynamics of guest proteins in liquid droplets.

Indexed as

Biomolecular CondensatesIntrinsically Disordered ProteinsMicroscopy, FluorescenceMolecular Dynamics SimulationMutationOrganellesPhase TransitionProtein FoldingProtein MultimerizationSingle Molecule ImagingTumor Suppressor Protein p53Intrinsically Disordered ProteinsTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID34588591
PMCPMC8481498
OpenAlexW3203395139

What OpenQuestion holds

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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 OpenQuestion graph.