{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang Z"],"funding":["Leverhulme Trust","British Heart Foundation","Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)","Medical Research Council","Royal Society","Wellcome Trust"],"pagination":["4090"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12046049"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["The biomechanical properties and responses of tissues underpin a variety important of physiological functions and pathologies. In striated muscle, the actin-binding protein filamin C (FLNC) is a key protein whose variants causative for a wide range of cardiomyopathies and musculoskeletal pathologies. FLNC is a multi-functional protein that interacts with a variety of partners, however, how it is regulated at the molecular level is not well understood. Here we investigate its interaction with HSPB7, a cardiac-specific molecular chaperone whose absence is embryonically lethal. We find that FLNC and HSPB7 interact in cardiac tissue under biomechanical stress, forming a strong hetero-dimer whose structure we solve by X-ray crystallography. Our quantitative analyses show that the hetero-dimer o"],"journal":["Nature communications"],"pubmed_title":["Filamin C dimerisation is regulated by HSPB7."],"pmcid":["PMC12046049"],"funding_grant_id":["FOR 2743 - FU339/11-2","FU339/13-1","MR/V009540/1","RE/13/1/30181","FS/12/40/29712","RPG-2021-246","FOR 2743, project P09 (WA1598/6)","201543/B/16/Z","AA/18/2/34218"],"pubmed_authors":["Alderson TR","Cao G","Saman D","Zimmermann J","Collier MP","Qiu X","Broadway-Stringer S","Ng JZY","Brem J","Wang Z","Hochberg GKA","Bolla JR","Azad AJ","McDonough MA","Djinovic-Carugo K","Sen N","Robinson CV","Song H","Schofield CJ","Rabe P","Gehmlich K","Allison TM","Hooper C","Furst DO","Warscheid B","Degiacomi MT","Benesch JLP"],"additional_accession":[]},"is_claimable":false,"name":"Filamin C dimerisation is regulated by HSPB7.","description":"The biomechanical properties and responses of tissues underpin a variety important of physiological functions and pathologies. In striated muscle, the actin-binding protein filamin C (FLNC) is a key protein whose variants causative for a wide range of cardiomyopathies and musculoskeletal pathologies. FLNC is a multi-functional protein that interacts with a variety of partners, however, how it is regulated at the molecular level is not well understood. Here we investigate its interaction with HSPB7, a cardiac-specific molecular chaperone whose absence is embryonically lethal. We find that FLNC and HSPB7 interact in cardiac tissue under biomechanical stress, forming a strong hetero-dimer whose structure we solve by X-ray crystallography. Our quantitative analyses show that the hetero-dimer o","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-02T20:56:29.582Z","creation":"2025-07-06T03:05:52.641Z"},"accession":"S-EPMC12046049","cross_references":{"pubmed":["40312381"],"doi":["10.1038/s41467-025-58889-x"]}}