{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zheng B"],"funding":["Henan Zhongyuan Medical Science and Technology Innovation Development Foundation","National Natural Science Foundation of China","National Key Research and Development Program of China","The Center for Advanced Interdisciplinary Science and Biomedicine of IHM","The China Postdoctoral Science Foundation"],"pagination":["442"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12715077"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["82(1)"],"pubmed_abstract":["Polarized cell growth necessitates the dynamic remodeling of the plasma membrane, a process requiring BAR domain-containing proteins. While classical BAR proteins, with their crescent-shaped structure, are well characterized, the mechanisms underlying the localization and function of elongated F-BAR proteins remain unclear. Here, we demonstrate that the F-BAR domains of the fission yeast proteins Rga7 and Rga8 undergo liquid-liquid phase separation (LLPS). These domains form oligomers via hydrophobic interactions and assemble into condensates through electrostatic interactions mediated by the charged residues at their tips. Mutants deficient in phase separation fail to localize properly at cell poles, leading to defective polar distribution of key regulators, including the Rho GTPases, the"],"journal":["Cellular and molecular life sciences : CMLS"],"pubmed_title":["Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity."],"pmcid":["PMC12715077"],"funding_grant_id":["92354304, 32470725","2023TQ0342","QYPY20220003","ZYYC202401ZD","2022YFA1303100","32300563"],"pubmed_authors":["Liu X","Fu C","Wang C","Zhang X","Xiang S","Zheng S","Zheng B","Xu C","Lin Y","Wei W","Song X","Wang L"],"additional_accession":[]},"is_claimable":false,"name":"Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity.","description":"Polarized cell growth necessitates the dynamic remodeling of the plasma membrane, a process requiring BAR domain-containing proteins. While classical BAR proteins, with their crescent-shaped structure, are well characterized, the mechanisms underlying the localization and function of elongated F-BAR proteins remain unclear. Here, we demonstrate that the F-BAR domains of the fission yeast proteins Rga7 and Rga8 undergo liquid-liquid phase separation (LLPS). These domains form oligomers via hydrophobic interactions and assemble into condensates through electrostatic interactions mediated by the charged residues at their tips. Mutants deficient in phase separation fail to localize properly at cell poles, leading to defective polar distribution of key regulators, including the Rho GTPases, the","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-06T05:31:05.836Z","creation":"2026-05-26T03:12:21.084Z"},"accession":"S-EPMC12715077","cross_references":{"pubmed":["41413653"],"doi":["10.1007/s00018-025-05977-2"]}}