Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.
cochlear amplification
cryo-electron microscopy
human
hydrogen exchange
mass spectrometry
molecular biophysics
protein folding
structural biology
voltage sensing
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
06 Dec 2023
06 Dec 2023
Historique:
medline:
7
12
2023
pubmed:
6
12
2023
entrez:
6
12
2023
Statut:
epublish
Résumé
Prestin responds to transmembrane voltage fluctuations by changing its cross-sectional area, a process underlying the electromotility of outer hair cells and cochlear amplification. Prestin belongs to the SLC26 family of anion transporters yet is the only member capable of displaying electromotility. Prestin's voltage-dependent conformational changes are driven by the putative displacement of residue R399 and a set of sparse charged residues within the transmembrane domain, following the binding of a Cl
Identifiants
pubmed: 38054956
doi: 10.7554/eLife.89635
pii: 89635
pmc: PMC10699807
doi:
pii:
Substances chimiques
Anions
0
Lipid Bilayers
0
Membrane Transport Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIDCD NIH HHS
ID : R01 DC019833
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM148233
Pays : United States
Organisme : NIGMS NIH HHS
ID : 1R35GM148233
Pays : United States
Informations de copyright
© 2023, Lin et al.
Déclaration de conflit d'intérêts
XL, PH, NB, NF, EP, TS No competing interests declared
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