{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kuwabara MF"],"funding":["MEXT | Japan Society for the Promotion of Science","Deutscher Akademischer Austauschdienst","Deutsche Forschungsgemeinschaft"],"pagination":["7145"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10628124"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["The outstanding acuity of the mammalian ear relies on cochlear amplification, an active mechanism based on the electromotility (eM) of outer hair cells. eM is a piezoelectric mechanism generated by little-understood, voltage-induced conformational changes of the anion transporter homolog prestin (SLC26A5). We used a combination of molecular dynamics (MD) simulations and biophysical approaches to identify the structural dynamics of prestin that mediate eM. MD simulations showed that prestin samples a vast conformational landscape with expanded (ES) and compact (CS) states beyond previously reported prestin structures. Transition from CS to ES is dominated by the translational-rotational movement of prestin's transport domain, akin to elevator-type substrate translocation by related solute c"],"journal":["Nature communications"],"pubmed_title":["Elevator-like movements of prestin mediate outer hair cell electromotility."],"pmcid":["PMC10628124"],"funding_grant_id":["OL 240/8-1","OL 240/4-2","19J20169","MA 7525/2-1"],"pubmed_authors":["Haddad BG","Hartmann J","Longo P","Oliver D","Fuß A","Huckschlag BM","Kuwabara MF","Lenz-Schwab D","Berger TK","Machtens JP","Questino A"],"additional_accession":[]},"is_claimable":false,"name":"Elevator-like movements of prestin mediate outer hair cell electromotility.","description":"The outstanding acuity of the mammalian ear relies on cochlear amplification, an active mechanism based on the electromotility (eM) of outer hair cells. eM is a piezoelectric mechanism generated by little-understood, voltage-induced conformational changes of the anion transporter homolog prestin (SLC26A5). We used a combination of molecular dynamics (MD) simulations and biophysical approaches to identify the structural dynamics of prestin that mediate eM. MD simulations showed that prestin samples a vast conformational landscape with expanded (ES) and compact (CS) states beyond previously reported prestin structures. Transition from CS to ES is dominated by the translational-rotational movement of prestin's transport domain, akin to elevator-type substrate translocation by related solute c","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2026-05-28T22:28:52.506Z","creation":"2025-02-19T00:01:20.441Z"},"accession":"S-EPMC10628124","cross_references":{"pubmed":["37932294"],"doi":["10.1038/s41467-023-42489-8"]}}