{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schulten A"],"funding":["European Research Council","Medical Research Council","The Royal Society","Wellcome Trust","Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["3321-3332.e5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7618248"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["85(17)"],"pubmed_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"],"journal":["Molecular cell"],"pubmed_title":["VEL-dependent polymerization maintains the chromatin association of Polycomb proteins for the switch to epigenetic silencing."],"pmcid":["PMC7618248"],"funding_grant_id":["EPISWITCH-833254","MC_U105192713","MC_U105192715","833254","EP/W024063/1","RP\\\\R1\\\\180002","BB/P013511/1","BB/J004588/1","225217/Z/22/Z","210654/Z/18/Z","EP/T002166/1","EP/T00214X/1","210654"],"pubmed_authors":["Jang GJ","Leake MC","Dean C","Schulten A","Payne-Dwyer A","Fiedler M","Bienz M","Nielsen ML","Mateo-Bonmati E"],"additional_accession":[]},"is_claimable":false,"name":"VEL-dependent polymerization maintains the chromatin association of Polycomb proteins for the switch to epigenetic silencing.","description":"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","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-04T11:02:15.389Z","creation":"2026-05-08T03:10:57.936Z"},"accession":"S-EPMC7618248","cross_references":{"pubmed":["40858112"],"doi":["10.1016/j.molcel.2025.08.002"]}}