{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dufrancais O"],"funding":["Fondation Toulouse Cancer Santé","NIAID NIH HHS","European Molecular Biology Laboratory","French National Research Agency","Institut National de la Santé et de la Recherche Médicale","Fondation pour la recherche contre le cancer","CIHR","Foundation F. Initiativas par Fondation Fonroga Toulouse","INSERM","Toulouse Université Paul Sabatier","La Ligue contre le Cancer","Université Toulouse III - Paul Sabatier (UT3)","National Health & Medical Research Council of Australia","Centre National de la Recherche Scientifique","Fondation pour la Recherche Médicale","NIAMS NIH HHS","Wellcome Trust","Toulouse Université, La Ligue contre le cancer par Toulouse Université, CARe doctoral school","NIGMS NIH HHS","NIH HHS"],"pagination":["e202409169"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12558046"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["224(11)"],"pubmed_abstract":["Cell-cell fusion is an evolutionarily conserved process that is essential for many functions, including the formation of bone-resorbing multinucleated osteoclasts. Osteoclast multinucleation involves dynamic interactions between the actin cytoskeleton and the plasma membrane that are still poorly characterized. We found that moesin, a cytoskeletal linker protein member of the Ezrin, radixin, and moesin (ERM) protein family, plays a critical role in both osteoclast fusion and function. Moesin inhibition favors osteoclast multinucleation as well as HIV-1- and inflammation-induced cell fusion. Accordingly, moesin depletion decreases membrane-to-cortex attachment and enhances the formation of tunneling nanotubes, F-actin-based intercellular bridges triggering cell-cell fusion. In addition, moe"],"journal":["The Journal of cell biology"],"pubmed_title":["Moesin controls cell-cell fusion and osteoclast function."],"pmcid":["PMC12558046"],"funding_grant_id":["P30 AR069619","EQU202303016313","ANR-18-EURE-0003","ANR DFG 2020 JA-3038/2-1","APP2029078","APP2020097","ANR16-CE13-0005-01","ANR-10-INBS-04","PJT-1620109","ANR-20-CE14-0037","R01 AI147118","K12 GM081259","2K12GM081259-16"],"pubmed_authors":["Plozza M","Halper J","Sanchez T","Dufrancais O","Blin-Wakkach C","Ben Neji M","Bordignon PJ","Juzans M","Arnaud G","Burkhardt JK","Carreno S","Maridonneau-Parini I","Pavlos NJ","Diz-Munoz A","Boerckel JD","Verollet C","Raynaud-Messina B","Mascarau R","Gence R","Bergert M","Monard SC","Verdys P","Lagarrigue F","Metais A","Panebianco CJ","Poincloux R","Le Cabec V"],"additional_accession":[]},"is_claimable":false,"name":"Moesin controls cell-cell fusion and osteoclast function.","description":"Cell-cell fusion is an evolutionarily conserved process that is essential for many functions, including the formation of bone-resorbing multinucleated osteoclasts. Osteoclast multinucleation involves dynamic interactions between the actin cytoskeleton and the plasma membrane that are still poorly characterized. We found that moesin, a cytoskeletal linker protein member of the Ezrin, radixin, and moesin (ERM) protein family, plays a critical role in both osteoclast fusion and function. Moesin inhibition favors osteoclast multinucleation as well as HIV-1- and inflammation-induced cell fusion. Accordingly, moesin depletion decreases membrane-to-cortex attachment and enhances the formation of tunneling nanotubes, F-actin-based intercellular bridges triggering cell-cell fusion. In addition, moe","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-07-15T14:31:42.152Z","creation":"2026-07-06T03:08:46.593Z"},"accession":"S-EPMC12558046","cross_references":{"pubmed":["41143651"],"doi":["10.1083/jcb.202409169"]}}