Evidence map›Paper›PMID 37756159›Full record

ArticleCell reports2023

Principles of assembly and regulation of condensates of Polycomb repressive complex 1 through phase separation.

Kyle Brown, Pin Yu Chew, Steven Ingersoll, Jorge R Espinosa, Anne Aguirre, Axel Espinoza, Joey Wen, Kalkidan Astatike, Tatiana G Kutateladze, Rosana Collepardo-Guevara and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Kyle BrownDepartment of Chemistry, University of Colorado Denver, Denver, CO 80217-3364, USA.
Pin Yu ChewYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Steven IngersollDepartment of Chemistry, University of Colorado Denver, Denver, CO 80217-3364, USA.
Jorge R EspinosaDepartment of Physics, University of Cambridge, Cambridge CB3 0HE, UK.
Anne AguirreYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Axel EspinozaDepartment of Chemistry, University of Colorado Denver, Denver, CO 80217-3364, USA.
Joey WenDepartment of Chemistry, University of Colorado Denver, Denver, CO 80217-3364, USA.
Kalkidan AstatikeDepartment of Chemistry, University of Colorado Denver, Denver, CO 80217-3364, USA.
Tatiana G KutateladzeDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Rosana Collepardo-GuevaraYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK; Department of Physics, University of Cambridge, Cambridge CB3 0HE, UK; Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK. Electronic address: rc597@cam.ac.uk.
Xiaojun RenDepartment of Chemistry, University of Colorado Denver, Denver, CO 80217-3364, USA; Department of Integrative Biology, University of Colorado Denver, Denver, CO 80217-3364, USA. Electronic address: xiaojun.ren@ucdenver.edu.
University of Colorado Denver · USUniversity of Cambridge · GBUniversity of Denver · US

Funding

Spatial Organization of Epigenetic Complexes and ChromatinR01GM135286 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI PHIEL, CHRISTOPHER J · 2019 to 2022
$1.3M
NIGMS NIH HHS R01 GM135286
6 · The paper itself

Abstract

Polycomb repressive complex 1 (PRC1) undergoes phase separation to form Polycomb condensates that are multi-component hubs for silencing Polycomb target genes. In this study, we demonstrate that formation and regulation of PRC1 condensates are consistent with the scaffold-client model, where the Chromobox 2 (CBX2) protein behaves as the scaffold while the other PRC1 proteins are clients. Such clients induce a re-entrant phase transition of CBX2 condensates. The composition of the multi-component PRC1 condensates (1) determines the dynamic properties of the scaffold protein; (2) selectively promotes the formation of CBX4-PRC1 condensates while dissolving condensates of CBX6-, CBX7-, and CBX8-PRC1; and (3) controls the enrichment of CBX4-, CBX7-, and CBX8-PRC1 in CBX2-PRC1 condensates and the exclusion of CBX6-PRC1 from CBX2-PRC1 condensates. Our findings uncover how multi-component PRC1 condensates are assembled via an intricate scaffold-client mechanism whereby the properties of the PRC1 condensates are sensitively regulated by its composition and stoichiometry.

Indexed as

Cell NucleusPolycomb Repressive Complex 1ChromatinHumansLigasesPolycomb-Group ProteinsCBX4 protein, humanCBX7 protein, humanCBX8 protein, humanChromatinLigasesPolycomb-Group ProteinsPolycomb Repressive Complex 1CBXchromatincoarse-grained modelcomposition-dependent phase separationCP: Molecular biologyliquid-liquid phase separationPolycomb repressive complexPRC1scaffold-client

Identifiers

PMID37756159
PMCPMC10862386
OpenAlexW4387045128

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.