Prestin at year 14

Progress and prospect

Research output: Contribution to journalReview article

19 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)25-35
Number of pages11
JournalHearing Research
Volume311
DOIs
StatePublished - 2014

Fingerprint

Outer Auditory Hair Cells
Anions
Proteins
Membrane Transport Proteins
Cochlea
Molecular Dynamics Simulation
Genomics
Site-Directed Mutagenesis
Computational Biology
Molecular Structure
Cell Movement
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Sensory Systems

Cite this

Prestin at year 14 : Progress and prospect. / He, David Z.; Lovas, Sándor; Ai, Yu; Li, Yi; Beisel, Kirk.

In: Hearing Research, Vol. 311, 2014, p. 25-35.

Research output: Contribution to journalReview article

@article{e4175988909446bfb7369da8d89497af,
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.",
author = "He, {David Z.} and S{\'a}ndor Lovas and Yu Ai and Yi Li and Kirk Beisel",
year = "2014",
doi = "10.1016/j.heares.2013.12.002",
language = "English",
volume = "311",
pages = "25--35",
journal = "Hearing Research",
issn = "0378-5955",
publisher = "Elsevier",

}

TY - JOUR

T1 - Prestin at year 14

T2 - Progress and prospect

AU - He, David Z.

AU - Lovas, Sándor

AU - Ai, Yu

AU - Li, Yi

AU - Beisel, Kirk

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84906512415&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84906512415&partnerID=8YFLogxK

U2 - 10.1016/j.heares.2013.12.002

DO - 10.1016/j.heares.2013.12.002

M3 - Review article

VL - 311

SP - 25

EP - 35

JO - Hearing Research

JF - Hearing Research

SN - 0378-5955

ER -