title: Prestin at year 14: progress and prospect.
abstract: Prestin, the motor protein of cochlear outer hair cells, was identified 14 years ago. Prestin-based outer hair cell motility is responsible for the exquisite sensitivity and frequency selectivity seen in the mammalian cochlea. Prestin is the 5th member of an eleven-member membrane transporter superfamily of SLC26A proteins. Unlike its paralogs, which are capable of transporting anions across the cell membrane, prestin primarily functions as a motor protein with unique capability of performing direct and reciprocal electromechanical conversion on microsecond time scale. Significant progress in the understanding of its structure and the molecular mechanism has been made in recent years using electrophysiological, biochemical, comparative genomics, structural bioinformatics, molecular dynamics simulation, site-directed mutagenesis and domain-swapping techniques. This article reviews recent advances of the structural and functional properties of prestin with focus on the areas that are critical but still controversial in understanding the molecular mechanism of how prestin works: The structural domains for voltage sensing and interaction with anions and for conformational change. Future research directions and potential application of prestin are also discussed. This article is part of a Special Issue entitled <Annual Reviews 2014>.
authors.affiliation: Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68175, USA; Neuroscience Center, Ningbo University School of Medicine, Ningbo 315211, China. Electronic address: hed@creighton.edu.
authors.forename: David Z Z
authors.initials: DZ
authors.lastname: He
authors.affiliation: Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68175, USA.
authors.forename: Sándor
authors.initials: S
authors.lastname: Lovas
authors.affiliation: Department of Otolaryngology, Shandong Provincial Hospital, Jinan 250021, PR China.
authors.forename: Yu
authors.initials: Y
authors.lastname: Ai
authors.affiliation: Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68175, USA; Department of Otolaryngology, Beijing Tongren Hospital, Beijing 100730, PR China.
authors.forename: Yi
authors.initials: Y
authors.lastname: Li
authors.affiliation: Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, NE 68175, USA.
authors.forename: Kirk W
authors.initials: KW
authors.lastname: Beisel
mesh_terms: D000161:Acoustic Stimulation; D000595:Amino Acid Sequence; D000818:Animals; D027321:Anion Transport Proteins / Q000737:chemistry / Q000378:metabolism*; D001307:Auditory Perception; D018072:Hair Cells, Auditory, Outer / Q000378:metabolism*; D006309:Hearing; D006801:Humans; D040542:Mechanotransduction, Cellular; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D000076988:Sulfate Transporters
chemical_list: D027321:Anion Transport Proteins; C498719:SLC26A5 protein, human; D000076988:Sulfate Transporters