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Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana

Author

Listed:
  • Jiangtao Guo

    (University of Texas Southwestern Medical Center)

  • Weizhong Zeng

    (University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Qingfeng Chen

    (University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Changkeun Lee

    (University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Liping Chen

    (University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Yi Yang

    (University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

  • Chunlei Cang

    (University of Pennsylvania)

  • Dejian Ren

    (University of Pennsylvania)

  • Youxing Jiang

    (University of Texas Southwestern Medical Center
    Howard Hughes Medical Institute, University of Texas Southwestern Medical Center)

Abstract

Two-pore channels (TPCs) contain two copies of a Shaker-like six-transmembrane (6-TM) domain in each subunit and are ubiquitously expressed in both animals and plants as organellar cation channels. Here we present the crystal structure of a vacuolar two-pore channel from Arabidopsis thaliana, AtTPC1, which functions as a homodimer. AtTPC1 activation requires both voltage and cytosolic Ca2+. Ca2+ binding to the cytosolic EF-hand domain triggers conformational changes coupled to the pair of pore-lining inner helices from the first 6-TM domains, whereas membrane potential only activates the second voltage-sensing domain, the conformational changes of which are coupled to the pair of inner helices from the second 6-TM domains. Luminal Ca2+ or Ba2+ can modulate voltage activation by stabilizing the second voltage-sensing domain in the resting state and shift voltage activation towards more positive potentials. Our Ba2+-bound AtTPC1 structure reveals a voltage sensor in the resting state, providing hitherto unseen structural insight into the general voltage-gating mechanism among voltage-gated channels.

Suggested Citation

  • Jiangtao Guo & Weizhong Zeng & Qingfeng Chen & Changkeun Lee & Liping Chen & Yi Yang & Chunlei Cang & Dejian Ren & Youxing Jiang, 2016. "Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana," Nature, Nature, vol. 531(7593), pages 196-201, March.
    • Handle: RePEc:nat:nature:v:531:y:2016:i:7593:d:10.1038_nature16446
    DOI: 10.1038/nature16446
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