Literature DB >> 20550895

Sensitivity of prestin-based membrane motor to membrane thickness.

Jie Fang1, Chisako Izumi, Kuni H Iwasa.   

Abstract

Prestin is the membrane protein in outer hair cells that harnesses electrical energy by changing its membrane area in response to changes in the membrane potential. To examine the effect of membrane thickness on this protein, phosphatidylcholine (PC) with various acyl-chain lengths were incorporated into the plasma membrane by using gamma-cyclodextrin. Incorporation of short chain PCs increased the linear capacitance and positively shifted the voltage dependence of prestin, up to 120 mV, in cultured cells. PCs with long acyl chains had the opposite effects. Because the linear capacitance is inversely related to the membrane thickness, these voltage shifts are attributable to membrane thickness. The corresponding voltage shifts of electromotility were observed in outer hair cells. These results demonstrate that electromotility is extremely sensitive to the thickness of the plasma membrane, presumably involving hydrophobic mismatch. These observations indicate that the extended state of the motor molecule, which is associated with the elongation of outer hair cells, has a conformation with a shorter hydrophobic height in the lipid bilayer. (c) 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20550895      PMCID: PMC2884244          DOI: 10.1016/j.bpj.2010.03.034

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


  34 in total

1.  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

2.  Piezoelectric reciprocal relationship of the membrane motor in the cochlear outer hair cell.

Authors:  Xiao-xia Dong; Mark Ospeck; Kuni H Iwasa
Journal:  Biophys J       Date:  2002-03       Impact factor: 4.033

3.  A two-state piezoelectric model for outer hair cell motility.

Authors:  K H Iwasa
Journal:  Biophys J       Date:  2001-11       Impact factor: 4.033

4.  Tension sensitivity of prestin: comparison with the membrane motor in outer hair cells.

Authors:  X-X Dong; K H Iwasa
Journal:  Biophys J       Date:  2004-02       Impact factor: 4.033

5.  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

6.  Voltage-dependent capacitance in lipid bilayers made from monolayers.

Authors:  O Alvarez; R Latorre
Journal:  Biophys J       Date:  1978-01       Impact factor: 4.033

7.  Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating.

Authors:  Eduardo Perozo; Anna Kloda; D Marien Cortes; Boris Martinac
Journal:  Nat Struct Biol       Date:  2002-09

Review 8.  Effects of membrane lipids on ion channel structure and function.

Authors:  Tommy S Tillman; Michael Cascio
Journal:  Cell Biochem Biophys       Date:  2003       Impact factor: 2.194

9.  Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol.

Authors:  Kakoli Mitra; Iban Ubarretxena-Belandia; Tomohiko Taguchi; Graham Warren; Donald M Engelman
Journal:  Proc Natl Acad Sci U S A       Date:  2004-03-11       Impact factor: 11.205

10.  Prestin-based outer hair cell motility is necessary for mammalian cochlear amplification.

Authors:  Peter Dallos; Xudong Wu; Mary Ann Cheatham; Jiangang Gao; Jing Zheng; Charles T Anderson; Shuping Jia; Xiang Wang; Wendy H Y Cheng; Soma Sengupta; David Z Z He; Jian Zuo
Journal:  Neuron       Date:  2008-05-08       Impact factor: 17.173

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  11 in total

1.  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

2.  The capacitance and electromechanical coupling of lipid membranes close to transitions: the effect of electrostriction.

Authors:  Thomas Heimburg
Journal:  Biophys J       Date:  2012-09-05       Impact factor: 4.033

3.  Membrane thickness sensitivity of prestin orthologs: the evolution of a piezoelectric protein.

Authors:  Chisako Izumi; Jonathan E Bird; Kuni H Iwasa
Journal:  Biophys J       Date:  2011-06-08       Impact factor: 4.033

4.  Molecular mechanism of prestin electromotive signal amplification.

Authors:  Jingpeng Ge; Johannes Elferich; Sepehr Dehghani-Ghahnaviyeh; Zhiyu Zhao; Marc Meadows; Henrique von Gersdorff; Emad Tajkhorshid; Eric Gouaux
Journal:  Cell       Date:  2021-08-13       Impact factor: 66.850

5.  Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility.

Authors:  Haon Futamata; Masahiro Fukuda; Rie Umeda; Keitaro Yamashita; Atsuhiro Tomita; Satoe Takahashi; Takafumi Shikakura; Shigehiko Hayashi; Tsukasa Kusakizako; Tomohiro Nishizawa; Kazuaki Homma; Osamu Nureki
Journal:  Nat Commun       Date:  2022-10-20       Impact factor: 17.694

6.  Coupling between outer hair cell electromotility and prestin sensor charge depends on voltage operating point.

Authors:  Joseph Santos-Sacchi; Winston J T Tan
Journal:  Hear Res       Date:  2021-10-30       Impact factor: 3.672

7.  Membrane cholesterol strongly influences confined diffusion of prestin.

Authors:  R I Kamar; L E Organ-Darling; R M Raphael
Journal:  Biophys J       Date:  2012-10-16       Impact factor: 4.033

8.  The conformational cycle of prestin underlies outer-hair cell electromotility.

Authors:  Navid Bavi; Michael David Clark; Gustavo F Contreras; Rong Shen; Bharat G Reddy; Wieslawa Milewski; Eduardo Perozo
Journal:  Nature       Date:  2021-10-25       Impact factor: 69.504

9.  Susceptibility of outer hair cells to cholesterol chelator 2-hydroxypropyl-β-cyclodextrine is prestin-dependent.

Authors:  Satoe Takahashi; Kazuaki Homma; Yingjie Zhou; Shinichi Nishimura; Chongwen Duan; Jessie Chen; Aisha Ahmad; Mary Ann Cheatham; Jing Zheng
Journal:  Sci Rep       Date:  2016-02-23       Impact factor: 4.379

10.  Diflunisal inhibits prestin by chloride-dependent mechanism.

Authors:  Guillaume Duret; Fred A Pereira; Robert M Raphael
Journal:  PLoS One       Date:  2017-08-17       Impact factor: 3.240

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