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Lipid-mediated prestin organization in outer hair cell membranes and its implications in sound amplification

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  • Sepehr Dehghani-Ghahnaviyeh

    (University of Illinois at Urbana-Champaign)

  • Zhiyu Zhao

    (University of Illinois at Urbana-Champaign)

  • Emad Tajkhorshid

    (University of Illinois at Urbana-Champaign)

Abstract

Prestin is a high-density motor protein in the outer hair cells (OHCs), whose conformational response to acoustic signals alters the shape of the cell, thereby playing a major role in sound amplification by the cochlea. Despite recent structures, prestin’s intimate interactions with the membrane, which are central to its function remained unresolved. Here, employing a large set (collectively, more than 0.5 ms) of coarse-grained molecular dynamics simulations, we demonstrate the impact of prestin’s lipid-protein interactions on its organization at densities relevant to the OHCs and its effectiveness in reshaping OHCs. Prestin causes anisotropic membrane deformation, which mediates a preferential membrane organization of prestin where deformation patterns by neighboring copies are aligned constructively. The resulting reduced membrane rigidity is hypothesized to maximize the impact of prestin on OHC reshaping. These results demonstrate a clear case of protein-protein cooperative communication in membrane, purely mediated by interactions with lipids.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34596-9
    DOI: 10.1038/s41467-022-34596-9
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    References listed on IDEAS

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    1. Jing Zheng & Weixing Shen & David Z. Z. He & Kevin B. Long & Laird D. Madison & Peter Dallos, 2000. "Prestin is the motor protein of cochlear outer hair cells," Nature, Nature, vol. 405(6783), pages 149-155, May.
    2. Yung-Ning Chang & Eva A. Jaumann & Katrin Reichel & Julia Hartmann & Dominik Oliver & Gerhard Hummer & Benesh Joseph & Eric R. Geertsma, 2019. "Structural basis for functional interactions in dimers of SLC26 transporters," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    3. 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.
    4. Navid Bavi & Michael David Clark & Gustavo F. Contreras & Rong Shen & Bharat G. Reddy & Wieslawa Milewski & Eduardo Perozo, 2021. "The conformational cycle of prestin underlies outer-hair cell electromotility," Nature, Nature, vol. 600(7889), pages 553-558, December.
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