Literature DB >> 18658219

Anion control of voltage sensing by the motor protein prestin in outer hair cells.

Volodymyr Rybalchenko1, Joseph Santos-Sacchi.   

Abstract

The outer hair cell from Corti's organ possesses voltage-dependent intramembranous molecular motors evolved from the SLC26 anion transporter family. The motor, identified as prestin (SLC26a5), is responsible for electromotility of outer hair cells and mammalian cochlear amplification, a process that heightens our auditory responsiveness. Here, we describe experiments designed to evaluate the effects of anions on the motor's voltage-sensor charge movement, focusing on prestin's voltage-dependent Boltzmann characteristics. We find that the nature of the anion, including species, valence, and structure, regulates characteristics of the charge movement, signifying that anions play a more complicated role than simple voltage sensing in cochlear amplification.

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Year:  2008        PMID: 18658219      PMCID: PMC2567960          DOI: 10.1529/biophysj.108.134197

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  43 in total

1.  X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.

Authors:  Raimund Dutzler; Ernest B Campbell; Martine Cadene; Brian T Chait; Roderick MacKinnon
Journal:  Nature       Date:  2002-01-17       Impact factor: 49.962

Review 2.  Ion-age molecular motors.

Authors:  R Meech; M Holley
Journal:  Nat Neurosci       Date:  2001-08       Impact factor: 24.884

Review 3.  Micro- and nanomechanics of the cochlear outer hair cell.

Authors:  W E Brownell; A A Spector; R M Raphael; A S Popel
Journal:  Annu Rev Biomed Eng       Date:  2001       Impact factor: 9.590

4.  Voltage-dependent changes in specific membrane capacitance caused by prestin, the outer hair cell lateral membrane motor.

Authors:  Joseph Santos-Sacchi; Enrique Navarrete
Journal:  Pflugers Arch       Date:  2002-02-20       Impact factor: 3.657

5.  Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein.

Authors:  D Oliver; D Z He; N Klöcker; J Ludwig; U Schulte; S Waldegger; J P Ruppersberg; P Dallos; B Fakler
Journal:  Science       Date:  2001-06-22       Impact factor: 47.728

6.  Cl- flux through a non-selective, stretch-sensitive conductance influences the outer hair cell motor of the guinea-pig.

Authors:  Volodymyr Rybalchenko; Joseph Santos-Sacchi
Journal:  J Physiol       Date:  2003-01-31       Impact factor: 5.182

Review 7.  Cochlear outer hair cell motility.

Authors:  Jonathan Ashmore
Journal:  Physiol Rev       Date:  2008-01       Impact factor: 37.312

8.  Prestin is the motor protein of cochlear outer hair cells.

Authors:  J Zheng; W Shen; D Z He; K B Long; L D Madison; P Dallos
Journal:  Nature       Date:  2000-05-11       Impact factor: 49.962

9.  Expression and localization of prestin and the sugar transporter GLUT-5 during development of electromotility in cochlear outer hair cells.

Authors:  I A Belyantseva; H J Adler; R Curi; G I Frolenkov; B Kachar
Journal:  J Neurosci       Date:  2000-12-15       Impact factor: 6.167

10.  Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier.

Authors:  M Charles Liberman; Jiangang Gao; David Z Z He; Xudong Wu; Shuping Jia; Jian Zuo
Journal:  Nature       Date:  2002-08-28       Impact factor: 49.962

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  33 in total

Review 1.  Molecular mechanism of pancreatic and salivary gland fluid and HCO3 secretion.

Authors:  Min Goo Lee; Ehud Ohana; Hyun Woo Park; Dongki Yang; Shmuel Muallem
Journal:  Physiol Rev       Date:  2012-01       Impact factor: 37.312

2.  Evidence that prestin has at least two voltage-dependent steps.

Authors:  Kazuaki Homma; Peter Dallos
Journal:  J Biol Chem       Date:  2010-11-11       Impact factor: 5.157

Review 3.  Chansporter complexes in cell signaling.

Authors:  Geoffrey W Abbott
Journal:  FEBS Lett       Date:  2017-08-02       Impact factor: 4.124

4.  Engineered pendrin protein, an anion transporter and molecular motor.

Authors:  Jie Tang; Jason L Pecka; Xiaodong Tan; Kirk W Beisel; David Z Z He
Journal:  J Biol Chem       Date:  2011-07-13       Impact factor: 5.157

5.  Chloride Anions Regulate Kinetics but Not Voltage-Sensor Qmax of the Solute Carrier SLC26a5.

Authors:  Joseph Santos-Sacchi; Lei Song
Journal:  Biophys J       Date:  2016-06-07       Impact factor: 4.033

6.  Conformational state-dependent anion binding in prestin: evidence for allosteric modulation.

Authors:  Lei Song; Joseph Santos-Sacchi
Journal:  Biophys J       Date:  2010-02-03       Impact factor: 4.033

7.  Disparities in voltage-sensor charge and electromotility imply slow chloride-driven state transitions in the solute carrier SLC26a5.

Authors:  Lei Song; Joseph Santos-Sacchi
Journal:  Proc Natl Acad Sci U S A       Date:  2013-02-19       Impact factor: 11.205

8.  Chloride-driven electromechanical phase lags at acoustic frequencies are generated by SLC26a5, the outer hair cell motor protein.

Authors:  Joseph Santos-Sacchi; Lei Song
Journal:  Biophys J       Date:  2014-07-01       Impact factor: 4.033

9.  The V499G/Y501H mutation impairs fast motor kinetics of prestin and has significance for defining functional independence of individual prestin subunits.

Authors:  Kazuaki Homma; Chongwen Duan; Jing Zheng; Mary Ann Cheatham; Peter Dallos
Journal:  J Biol Chem       Date:  2012-12-04       Impact factor: 5.157

10.  Prestin's anion transport and voltage-sensing capabilities are independent.

Authors:  Jun-Ping Bai; Alexei Surguchev; Simone Montoya; Peter S Aronson; Joseph Santos-Sacchi; Dhasakumar Navaratnam
Journal:  Biophys J       Date:  2009-04-22       Impact factor: 4.033

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