Evidence map›Paper›PMID 40441156›Full record

ArticleMolecular cell2025

A disordered linker in the Polycomb protein Polyhomeotic tunes phase separation and oligomerization.

Tim M Gemeinhardt, Roshan M Regy, Tien M Phan, Nanu Pal, Jyoti Sharma, Olga Senkovich, Andrea J Mendiola, Heather J Ledterman, Amy Henrickson, Daniel Lopes and 9 more

Abstract read
In one paragraph

Article in Molecular cell, 2025. 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
–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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. PAR-Driven Condensation Maintains Stalled Replication Fork Stability.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors.

Tim M GemeinhardtMontreal Clinical Research Institute (IRCM), Montreal, QC, Canada; Division of Experimental Medicine, McGill University, Montreal, QC, Canada.
Roshan M RegyArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.
Tien M PhanArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.
Nanu PalMontreal Clinical Research Institute (IRCM), Montreal, QC, Canada; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC, Canada.
Jyoti SharmaMontreal Clinical Research Institute (IRCM), Montreal, QC, Canada.
Olga SenkovichDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ, USA.
Andrea J MendiolaDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ, USA.
Heather J LedtermanDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ, USA.
Amy HenricksonDepartment of Chemistry and Biochemistry, The University of Lethbridge, Lethbridge, AB, Canada.
Daniel LopesDepartment of Chemistry and Biochemistry, City College of New York, New York, NY, USA.
Utkarsh KapoorDepartment of Chemical and Biomedical Engineering, University of Wyoming, Laramie, WY, USA.
Ashish BihaniMontreal Clinical Research Institute (IRCM), Montreal, QC, Canada; Division of Experimental Medicine, McGill University, Montreal, QC, Canada.
Djamouna SihouMontreal Clinical Research Institute (IRCM), Montreal, QC, Canada; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC, Canada.
Young C KimCenter for Materials Physics and Technology, Naval Research Laboratory, Washington, DC, USA.
David JeruzalmiDepartment of Chemistry and Biochemistry, City College of New York, New York, NY, USA; Ph.D. Program in Biochemistry, The Graduate Center of the City University of New York, New York, NY, USA; Ph.D. Program in Biology, The Graduate Center of the City University of New York, New York, NY, USA; Ph.D. Program in Chemistry, The Graduate Center of the City University of New York, New York, NY, USA.
Borries DemelerDepartment of Chemistry and Biochemistry, The University of Lethbridge, Lethbridge, AB, Canada; Department of Chemistry and Biochemistry, University of Montana, Missoula, MT, USA.
Chongwoo A KimDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ, USA.
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA; Department of Chemistry, Texas A&M University, College Station, TX, USA; Interdisciplinary Graduate Program in Genetics and Genomics, Texas A&M University, College Station, TX, USA. Electronic address: jeetain@tamu.edu.
Nicole J FrancisMontreal Clinical Research Institute (IRCM), Montreal, QC, Canada; Division of Experimental Medicine, McGill University, Montreal, QC, Canada; Department of Biochemistry and Molecular Medicine, University of Montreal, Montreal, QC, Canada. Electronic address: nicole.francis@ircm.qc.ca.

Funding

Development of an UltraScan Meta-Scheduler for HPC Job SubmissionR01GM120600 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Emre H. Brookes, BORRIES DEMELER · 2016 to 2026
$3.6M
Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
Multiscale Computational Models to Investigate the Role of Phase Separation in BiologyR35GM153388 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI Jeetain Mittal · 2024 to 2026
$1.3M
The role of SAM polymerization in Polycomb-dependent chromatin structuresR01GM114338 · NIGMS · MIDWESTERN UNIVERSITY · PI FRANCIS, NICOLE JANE, KIM, CHONGWOO A · 2016 to 2019
$1.0M
NIGMS NIH HHS R01 GM114338NIGMS NIH HHS R01 GM120600NIGMS NIH HHS R01 GM136917NIGMS NIH HHS R35 GM153388
6 · The paper itself

Abstract

Biomolecular condensates are increasingly recognized as key regulators of chromatin organization, yet how their formation and properties arise from protein sequences remains incompletely understood. Cross-species comparisons can reveal both conserved functions and significant evolutionary differences. Here, we integrate in vitro reconstitution, molecular dynamics simulations, and cell-based assays to examine how Drosophila and human variants of Polyhomeotic (Ph)-a subunit of the PRC1 chromatin regulatory complex-drive condensate formation through their sterile alpha motif (SAM) oligomerization domains. We identify divergent interactions between SAM and the disordered linker connecting it to the rest of Ph. These interactions enhance oligomerization and modulate both the formation and properties of reconstituted condensates. Oligomerization influences condensate dynamics but minimally impacts condensate formation. Linker-SAM interactions also affect condensate formation in Drosophila and human cells and growth in Drosophila imaginal discs. Our findings show how evolutionary changes in disordered linkers can fine-tune condensate properties, providing insights into sequence-function relationships.

Indexed as

DNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsPolycomb Repressive Complex 1AnimalsBiomolecular CondensatesCell Cycle ProteinsChromatinHumansImaginal DiscsMolecular Dynamics SimulationPhase SeparationProtein BindingProtein MultimerizationCell Cycle ProteinsChromatinDNA-Binding ProteinsDrosophila Proteinsph-d protein, DrosophilaPolycomb Repressive Complex 1PRC1 protein, humananalytical ultracentrifugationbiochemistrybiomolecular condensatesCRISPRDrosophilagene regulationintrinsically disordered regionsmolecular dynamics simulationsoligomerizationphase separationPolycombsterile alpha motif

Identifiers

PMID40441156
PMCPMC12145237

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.