Evidence map›Paper›PMID 40858112›Full record

ArticleMolecular cell2025

VEL-dependent polymerization maintains the chromatin association of Polycomb proteins for the switch to epigenetic silencing.

Anna Schulten, Geng-Jen Jang, Alex Payne-Dwyer, Marc Fiedler, Mathias L Nielsen, Eduardo Mateo-Bonmatí, Mariann Bienz, Mark C Leake, Caroline Dean

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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

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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

9 authors.

Anna SchultenDepartment of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK. Electronic address: anna.schulten@jic.ac.uk.
Geng-Jen JangDepartment of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK.
Alex Payne-DwyerSchool of Physics, Engineering and Technology, University of York, York YO10 5DD, UK; Department of Biology, University of York, York YO10 5DD, UK.
Marc FiedlerMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Mathias L NielsenDepartment of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK.
Eduardo Mateo-BonmatíDepartment of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK.
Mariann BienzMedical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Mark C LeakeSchool of Physics, Engineering and Technology, University of York, York YO10 5DD, UK; Department of Biology, University of York, York YO10 5DD, UK.
Caroline DeanDepartment of Cell and Developmental Biology, John Innes Centre, Norwich NR4 7UH, UK; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, UK. Electronic address: caroline.dean@jic.ac.uk.

Funding

Medical Research Council MC_U105192713Wellcome Trust
6 · The paper itself

Abstract

Multivalent protein-chromatin interactions facilitated by higher-order protein assemblies are emerging as a crucial theme in eukaryotic gene regulation. However, understanding the underlying mechanisms in their functional context remains challenging. Arabidopsis VEL proteins assemble biomolecular condensates by head-to-tail polymerization. Here, we dissect the role of VEL polymerization domains in conferring the epigenetic switch to Polycomb repressive complex 2 (PRC2) silencing at Arabidopsis FLOWERING LOCUS C (FLC). We show that VIN3 VEL polymerization produces higher-order nuclear VIN3 assemblies in vivo, which promote multivalent chromatin association and efficient H3K27me3 nucleation. VRN5 VEL polymerization, however, is not required unless a third homolog VEL1 is absent. The VRN5 VEL domain has different polymerization properties and is functionally unable to replace VIN3 VEL, but it is required to physically connect VIN3 with PRC2. This work reveals the combinatorial roles of VEL polymerization domains in maintaining the chromatin association of Polycomb proteins for the switch to epigenetic silencing.

Indexed as

ArabidopsisArabidopsis ProteinsChromatinEpigenesis, GeneticGene SilencingMADS Domain ProteinsPolycomb-Group ProteinsPolycomb Repressive Complex 2Gene Expression Regulation, PlantHistonesPlants, Genetically ModifiedPolymerizationProtein DomainsArabidopsis ProteinsAt5g10140 protein, ArabidopsisChromatinHistonesMADS Domain ProteinsPolycomb-Group ProteinsPolycomb Repressive Complex 2PRC2 protein, ArabidopsisepigeneticsFLChead-to-tail-polymerizationhigher-order protein assembliesPolycomb silencingPRC2 accessory proteinsvernalization

Identifiers

PMID40858112
PMCPMC7618248

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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.