{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ding M"],"funding":["NICHD NIH HHS","National Institute of Child Health and Human Development"],"pagination":["978-997.e25"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11863002"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["188(4)"],"pubmed_abstract":["Xist RNA initiates X inactivation as it spreads in cis across the chromosome. Here, we reveal a biophysical basis for its cis-limited diffusion. Xist RNA and HNRNPK together drive a liquid-liquid phase separation (LLPS) that encapsulates the chromosome. HNRNPK droplets pull on Xist and internalize the RNA. Once internalized, Xist induces a further phase transition and \"softens\" the HNRNPK droplet. Xist alters the condensate's deformability, adhesiveness, and wetting properties in vitro. Other Xist-interacting proteins are internalized and entrapped within the droplet, resulting in a concentration of Xist and protein partners within the condensate. We attribute LLPS to HNRNPK's RGG and Xist's repeat B (RepB) motifs. Mutating these motifs causes Xist diffusion, disrupts polycomb recruitment,"],"journal":["Cell"],"pubmed_title":["A biophysical basis for the spreading behavior and limited diffusion of Xist."],"pmcid":["PMC11863002"],"funding_grant_id":["R01 HD097665"],"pubmed_authors":["Jiang J","Lee JT","Wang D","Lappala A","Rivera C","Li P","Chen H","Weissbein U","Kesner B","Grimm NB","Ding M","Lou J"],"additional_accession":[]},"is_claimable":false,"name":"A biophysical basis for the spreading behavior and limited diffusion of Xist.","description":"Xist RNA initiates X inactivation as it spreads in cis across the chromosome. Here, we reveal a biophysical basis for its cis-limited diffusion. Xist RNA and HNRNPK together drive a liquid-liquid phase separation (LLPS) that encapsulates the chromosome. HNRNPK droplets pull on Xist and internalize the RNA. Once internalized, Xist induces a further phase transition and \"softens\" the HNRNPK droplet. Xist alters the condensate's deformability, adhesiveness, and wetting properties in vitro. Other Xist-interacting proteins are internalized and entrapped within the droplet, resulting in a concentration of Xist and protein partners within the condensate. We attribute LLPS to HNRNPK's RGG and Xist's repeat B (RepB) motifs. Mutating these motifs causes Xist diffusion, disrupts polycomb recruitment,","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-07-16T09:16:34.952Z","creation":"2026-07-09T10:46:49.885Z"},"accession":"S-EPMC11863002","cross_references":{"pubmed":["39824183"],"doi":["10.1016/j.cell.2024.12.004"]}}