Folding of prestin's anion-binding site and the mechanism of outer hair cell electromotility.

cochlear amplification cryo-electron microscopy human hydrogen exchange mass spectrometry molecular biophysics protein folding structural biology voltage sensing

Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
06 Dec 2023
Historique:
medline: 7 12 2023
pubmed: 6 12 2023
entrez: 6 12 2023
Statut: epublish

Résumé

Prestin responds to transmembrane voltage fluctuations by changing its cross-sectional area, a process underlying the electromotility of outer hair cells and cochlear amplification. Prestin belongs to the SLC26 family of anion transporters yet is the only member capable of displaying electromotility. Prestin's voltage-dependent conformational changes are driven by the putative displacement of residue R399 and a set of sparse charged residues within the transmembrane domain, following the binding of a Cl

Identifiants

pubmed: 38054956
doi: 10.7554/eLife.89635
pii: 89635
pmc: PMC10699807
doi:
pii:

Substances chimiques

Anions 0
Lipid Bilayers 0
Membrane Transport Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIDCD NIH HHS
ID : R01 DC019833
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM148233
Pays : United States
Organisme : NIGMS NIH HHS
ID : 1R35GM148233
Pays : United States

Informations de copyright

© 2023, Lin et al.

Déclaration de conflit d'intérêts

XL, PH, NB, NF, EP, TS No competing interests declared

Références

Trends Biochem Sci. 2020 Oct;45(10):906-918
pubmed: 32487353
Biophys J. 2006 Jun 1;90(11):4035-45
pubmed: 16565043
Biophys J. 2002 Mar;82(3):1254-9
pubmed: 11867442
Nat Methods. 2019 Jul;16(7):595-602
pubmed: 31249422
Nature. 2002 Sep 19;419(6904):300-4
pubmed: 12239568
Hear Res. 2022 Sep 15;423:108525
pubmed: 35599199
J Neurosci. 2014 Jan 22;34(4):1325-32
pubmed: 24453323
Elife. 2019 Jul 24;8:
pubmed: 31339488
IUCrJ. 2021 Sep 07;8(Pt 6):867-877
pubmed: 34804541
Nature. 2021 Dec;600(7889):553-558
pubmed: 34695838
Biophys J. 2009 Apr 22;96(8):3179-86
pubmed: 19383462
J Physiol. 2003 Mar 15;547(Pt 3):873-91
pubmed: 12562920
Elife. 2023 Dec 06;12:
pubmed: 38054956
Nat Commun. 2022 Jan 12;13(1):290
pubmed: 35022426
Phys Chem Chem Phys. 2017 Feb 15;19(7):5028-5036
pubmed: 28165082
Proc Natl Acad Sci U S A. 2007 May 15;104(20):8311-5
pubmed: 17494761
J Am Soc Mass Spectrom. 2021 Dec 1;32(12):2711-2727
pubmed: 34749499
Cell. 2021 Sep 2;184(18):4669-4679.e13
pubmed: 34390643
Science. 2001 Jun 22;292(5525):2340-3
pubmed: 11423665
J Mol Biol. 1993 Dec 5;234(3):779-815
pubmed: 8254673
J Biol Chem. 2008 Aug 15;283(33):22473-81
pubmed: 18567583
Nat Methods. 2017 Mar;14(3):290-296
pubmed: 28165473
Sci Rep. 2019 May 3;9(1):6874
pubmed: 31053797
PLoS Comput Biol. 2018 Dec 27;14(12):e1006342
pubmed: 30589846
Biochem Soc Trans. 2020 Jun 30;48(3):1227-1241
pubmed: 32369548
Proc Natl Acad Sci U S A. 2007 May 1;104(18):7693-8
pubmed: 17442754
Protein Sci. 2022 Jan;31(1):209-220
pubmed: 34716622
PLoS One. 2013;8(1):e54388
pubmed: 23342145
Acta Crystallogr D Struct Biol. 2018 Jun 1;74(Pt 6):531-544
pubmed: 29872004
J Mol Biol. 2003 Oct 31;333(4):721-45
pubmed: 14568533
Sci Adv. 2018 May 11;4(5):eaar6179
pubmed: 29756037
Anal Chem. 2019 Jul 2;91(13):8008-8016
pubmed: 31099554
EMBO J. 2011 Jun 24;30(14):2793-804
pubmed: 21701557
PLoS Comput Biol. 2018 Dec 27;14(12):e1006578
pubmed: 30589834
Protein Sci. 2022 Sep;31(9):e4402
pubmed: 36040258
Biophys J. 2010 Feb 3;98(3):371-6
pubmed: 20141749
Nat Commun. 2018 Oct 8;9(1):4151
pubmed: 30297844
Protein Sci. 2021 Jan;30(1):70-82
pubmed: 32881101
Cell Discov. 2020 Aug 10;6:55
pubmed: 32818062
J Cell Sci. 2012 Feb 15;125(Pt 4):1039-47
pubmed: 22399806
Proteins. 1993 Sep;17(1):75-86
pubmed: 8234246
Prog Biophys Mol Biol. 2019 May;143:5-12
pubmed: 30553754
Proc Natl Acad Sci U S A. 2022 May 17;119(20):e2119436119
pubmed: 35549554
Biophys J. 2008 Nov 1;95(9):4439-47
pubmed: 18658219
Integr Comp Biol. 2018 Aug 1;58(2):282-300
pubmed: 29917041
Biochem J. 2021 Dec 22;478(24):4169-4185
pubmed: 34783343
J Am Chem Soc. 2010 Jul 21;132(28):9513-5
pubmed: 20578693
Nat Commun. 2022 Mar 31;13(1):1709
pubmed: 35361752
Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2595-600
pubmed: 19196963
J Am Soc Mass Spectrom. 2018 Sep;29(9):1936-1939
pubmed: 30022340
Biophys J. 2009 Jan;96(2):739-47
pubmed: 19167318
J Physiol. 2006 Oct 1;576(Pt 1):37-42
pubmed: 16873410
Acta Crystallogr D Biol Crystallogr. 2015 Jan 1;71(Pt 1):136-53
pubmed: 25615868
Nat Commun. 2014 Apr 08;5:3622
pubmed: 24710176
Anal Chem. 2021 Sep 28;93(38):12840-12847
pubmed: 34523340
J Am Soc Mass Spectrom. 2006 Nov;17(11):1498-1509
pubmed: 16875839

Auteurs

Xiaoxuan Lin (X)

Center for Mechanical Excitability, The University of Chicago, Chicago, United States.
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.

Patrick R Haller (PR)

Center for Mechanical Excitability, The University of Chicago, Chicago, United States.
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.

Navid Bavi (N)

Center for Mechanical Excitability, The University of Chicago, Chicago, United States.
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.

Nabil Faruk (N)

Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.

Eduardo Perozo (E)

Center for Mechanical Excitability, The University of Chicago, Chicago, United States.
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.
Institute for Neuroscience, The University of Chicago, Chicago, United States.
Institute for Biophysical Dynamics, The University of Chicago, Chicago, United States.

Tobin R Sosnick (TR)

Center for Mechanical Excitability, The University of Chicago, Chicago, United States.
Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, United States.
Institute for Biophysical Dynamics, The University of Chicago, Chicago, United States.
Prizker School for Molecular Engineering, The University of Chicago, Chicago, United States.

Articles similaires

Animals Stereocilia Mice Mice, Knockout Noise
Adenosine Triphosphate Adenosine Diphosphate Mitochondrial ADP, ATP Translocases Binding Sites Mitochondria

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics

Classifications MeSH