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Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters

Author

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  • Dmitry Gorbunov

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Mattia Sturlese

    (University of Padua, via Marzolo 1)

  • Florian Nies

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Murielle Kluge

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Massimo Bellanda

    (University of Padua, via Marzolo 1)

  • Roberto Battistutta

    (University of Padua, via Marzolo 1
    Venetian Institute for Molecular Medicine (VIMM), via Orus 2)

  • Dominik Oliver

    (Institute of Physiology and Pathophysiology, Philipps University)

Abstract

Prestin (SLC26A5) is a member of the SLC26/SulP anion transporter family. Its unique quasi-piezoelectric mechanical activity generates fast cellular motility of cochlear outer hair cells, a key process underlying active amplification in the mammalian ear. Despite its established physiological role, it is essentially unknown how prestin can generate mechanical force, since structural information on SLC26/SulP proteins is lacking. Here we derive a structural model of prestin and related transporters by combining homology modelling, MD simulations and cysteine accessibility scanning. Prestin’s transmembrane core region is organized in a 7+7 inverted repeat architecture. The model suggests a central cavity as the substrate-binding site located midway of the anion permeation pathway, which is supported by experimental solute accessibility and mutational analysis. Anion binding to this site also controls the electromotile activity of prestin. The combined structural and functional data provide a framework for understanding electromotility and anion transport by SLC26 transporters.

Suggested Citation

  • Dmitry Gorbunov & Mattia Sturlese & Florian Nies & Murielle Kluge & Massimo Bellanda & Roberto Battistutta & Dominik Oliver, 2014. "Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters," Nature Communications, Nature, vol. 5(1), pages 1-13, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4622
    DOI: 10.1038/ncomms4622
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    Cited by:

    1. Makoto F. Kuwabara & Bassam G. Haddad & Dominik Lenz-Schwab & Julia Hartmann & Piersilvio Longo & Britt-Marie Huckschlag & Anneke Fuß & Annalisa Questino & Thomas K. Berger & Jan-Philipp Machtens & Do, 2023. "Elevator-like movements of prestin mediate outer hair cell electromotility," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Sepehr Dehghani-Ghahnaviyeh & Zhiyu Zhao & Emad Tajkhorshid, 2022. "Lipid-mediated prestin organization in outer hair cell membranes and its implications in sound amplification," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Haon Futamata & Masahiro Fukuda & Rie Umeda & Keitaro Yamashita & Atsuhiro Tomita & Satoe Takahashi & Takafumi Shikakura & Shigehiko Hayashi & Tsukasa Kusakizako & Tomohiro Nishizawa & Kazuaki Homma &, 2022. "Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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