Evidence map›Paper›PMID 39046778›Full record

ArticleMolecular biology of the cell2024

Measurement of solubility product reveals the interplay of oligomerization and self-association for defining condensate formation.

Aniruddha Chattaraj, Zeynep Baltaci, Steve Chung, Bruce J Mayer, Leslie M Loew, Jonathon A Ditlev

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2024. 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. Article
  2. Article
  3. Protein interactions, calcium, phosphorylation, and cholesterol modulate CFTR cluster formation on membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Aniruddha ChattarajR. D. Berlin Center for Cell Analysis and Modeling, University of Connecticut School of Medicine, Farmington, CT 06030.
Zeynep BaltaciProgram in Molecular Medicine, Toronto, ON M5G 1E8, Canada.
Steve ChungProgram in Molecular Medicine, Toronto, ON M5G 1E8, Canada.
Bruce J MayerR. D. Berlin Center for Cell Analysis and Modeling, University of Connecticut School of Medicine, Farmington, CT 06030.
Leslie M LoewR. D. Berlin Center for Cell Analysis and Modeling, University of Connecticut School of Medicine, Farmington, CT 06030.ORCID 0000-0002-1851-4646
Jonathon A DitlevProgram in Molecular Medicine, Toronto, ON M5G 1E8, Canada.ORCID 0000-0001-8287-7700

Funding

Mechanistic Modeling of Cellular SystemsR24GM137787 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI Pedro Mendes, Ion I. Moraru · 2020 to 2026
$8.9M
Mesoscale spatial kinetic modeling of cell systemsR01GM132859 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI LOEW, LESLIE M · 2019 to 2022
$1.4M
NIGMS NIH HHS R01 GM132859NIGMS NIH HHS R24 GM137787
6 · The paper itself

Abstract

Cellular condensates often consist of 10s to 100s of distinct interacting molecular species. Because of the complexity of these interactions, predicting the point at which they will undergo phase separation is daunting. Using experiments and computation, we therefore studied a simple model system consisting of polySH3 and polyPRM designed for pentavalent heterotypic binding. We tested whether the peak solubility product, or the product of the dilute phase concentration of each component, is a predictive parameter for the onset of phase separation. Titrating up equal total concentrations of each component showed that the maximum solubility product does approximately coincide with the threshold for phase separation in both experiments and models. However, we found that measurements of dilute phase concentration include small oligomers and monomers; therefore, a quantitative comparison of the experiments and models required inclusion of small oligomers in the model analysis. Even with the inclusion of small polyPRM and polySH3 oligomers, models did not predict experimental results. This led us to perform dynamic light scattering experiments, which revealed homotypic binding of polyPRM. Addition of this interaction to our model recapitulated the experimentally observed asymmetry. Thus, comparing experiments with simulation reveals that the solubility product can be predictive of the interactions underlying phase separation, even if small oligomers and low affinity homotypic interactions complicate the analysis.

Indexed as

SolubilityBiomolecular CondensatesHistonesProtein MultimerizationHistones

Identifiers

PMID39046778
PMCPMC11449392

What OpenQuestion holds

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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.