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Structural basis for functional interactions in dimers of SLC26 transporters

Author

Listed:
  • Yung-Ning Chang

    (Goethe University Frankfurt)

  • Eva A. Jaumann

    (Goethe University Frankfurt)

  • Katrin Reichel

    (Max Planck Institute of Biophysics)

  • Julia Hartmann

    (Philipps University)

  • Dominik Oliver

    (Philipps University
    Philipps University)

  • Gerhard Hummer

    (Max Planck Institute of Biophysics
    Goethe University Frankfurt)

  • Benesh Joseph

    (Goethe University Frankfurt
    Goethe University Frankfurt)

  • Eric R. Geertsma

    (Goethe University Frankfurt)

Abstract

The SLC26 family of transporters maintains anion equilibria in all kingdoms of life. The family shares a 7 + 7 transmembrane segments inverted repeat architecture with the SLC4 and SLC23 families, but holds a regulatory STAS domain in addition. While the only experimental SLC26 structure is monomeric, SLC26 proteins form structural and functional dimers in the lipid membrane. Here we resolve the structure of an SLC26 dimer embedded in a lipid membrane and characterize its functional relevance by combining PELDOR/DEER distance measurements and biochemical studies with MD simulations and spin-label ensemble refinement. Our structural model reveals a unique interface different from the SLC4 and SLC23 families. The functionally relevant STAS domain is no prerequisite for dimerization. Characterization of heterodimers indicates that protomers in the dimer functionally interact. The combined structural and functional data define the framework for a mechanistic understanding of functional cooperativity in SLC26 dimers.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10001-w
    DOI: 10.1038/s41467-019-10001-w
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    Cited by:

    1. 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.
    2. 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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