Evidence map›Paper›PMID 34677123›Full record

ArticleeLife2021

Physical observables to determine the nature of membrane-less cellular sub-compartments.

Mathias L Heltberg, Judith Miné-Hattab, Angela Taddei, Aleksandra M Walczak, Thierry Mora

Abstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Multi-Scale Imaging of the Dynamic Organization of Chromatin.International journal of molecular sciences · 2023
    Review
  5. HP1-driven phase separation recapitulates the thermodynamics and kinetics of heterochromatin condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Review
  8. Review
  9. Protein diffusion inScience advances · 2022
    Article
  10. Stochastic particle unbinding modulates growth dynamics and size of transcription factor condensates in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Multi-scale dynamics of heterochromatin repair.Current opinion in genetics & development · 2021
    Review
  12. Article
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

5 authors.

Mathias L HeltbergLaboratoire de physique de l'École normale supérieure, CNRS, PSL University, Sorbonne Université, and Université de Paris, Paris, France.ORCID 0000-0002-9699-4075
Judith Miné-HattabInstitut Curie, CNRS, PSL University, Sorbonne Université, Paris, France.ORCID 0000-0001-9986-4092
Angela TaddeiInstitut Curie, CNRS, PSL University, Sorbonne Université, Paris, France.ORCID 0000-0002-3217-0739
Aleksandra M WalczakLaboratoire de physique de l'École normale supérieure, CNRS, PSL University, Sorbonne Université, and Université de Paris, Paris, France.ORCID 0000-0002-2686-5702
Thierry MoraLaboratoire de physique de l'École normale supérieure, CNRS, PSL University, Sorbonne Université, and Université de Paris, Paris, France.ORCID 0000-0002-5456-9361

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spatial organization of complex biochemical reactions is essential for the regulation of cellular processes. Membrane-less structures called foci containing high concentrations of specific proteins have been reported in a variety of contexts, but the mechanism of their formation is not fully understood. Several competing mechanisms exist that are difficult to distinguish empirically, including liquid-liquid phase separation, and the trapping of molecules by multiple binding sites. Here, we propose a theoretical framework and outline observables to differentiate between these scenarios from single molecule tracking experiments. In the binding site model, we derive relations between the distribution of proteins, their diffusion properties, and their radial displacement. We predict that protein search times can be reduced for targets inside a liquid droplet, but not in an aggregate of slowly moving binding sites. We use our results to reject the multiple binding site model for Rad52 foci, and find a picture consistent with a liquid-liquid phase separation. These results are applicable to future experiments and suggest different biological roles for liquid droplet and binding site foci.

Indexed as

Cell MembraneDiffusionModels, BiologicalProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiae Proteinscellular fociliquid dropletliquid-liquid phase separationmembrane-less sub-compartmentsphysics of living systemspolymer binding modelS. cerevisiae

Identifiers

PMID34677123
PMCPMC8598233

What OpenQuestion holds

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LicenceCC BY
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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.