title: Prestin and the good vibrations.
abstract: In a recent paper published in the Biochemical Journal, Lolli et al. presented evidence that the C-terminal STAS (sulfate transporter and anti-sigma factor antagonist) domain of the motor protein prestin possesses an anion-binding site. This discovery might shed light on an aspect of the function of this mysterious and fascinating protein that is crucial for the human hearing system.
authors.affiliation: University of Strathclyde, Strathclyde Institute of Pharmacy and Biomedical Sciences, 161 Cathedral Street, Glasgow, G40RE, United Kingdom.
authors.forename: Anna Sofia
authors.initials: AS
authors.lastname: Birke
authors.affiliation: University of Strathclyde, Strathclyde Institute of Pharmacy and Biomedical Sciences, 161 Cathedral Street, Glasgow, G40RE, United Kingdom arnaud.javelle@strath.ac.uk.
authors.forename: Arnaud
authors.initials: A
authors.lastname: Javelle
mesh_terms: D000818:Animals; D027321:Anion Transport Proteins / Q000502:physiology*; D006309:Hearing / Q000502:physiology; D006801:Humans; D000076988:Sulfate Transporters
chemical_list: D027321:Anion Transport Proteins; C498719:SLC26A5 protein, human; D000076988:Sulfate Transporters
keywords: SLC26A5; STAS domain; cochlea; hearing system; outer hair cell; prestin