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

Jiangtao Guo, Weizhong Zeng, Qingfeng Chen, Changkeun Lee, Liping Chen, Yi Yang, Chunlei Cang, Dejian Ren and Youxing Jiang ()
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Jiangtao Guo: University of Texas Southwestern Medical Center
Weizhong Zeng: University of Texas Southwestern Medical Center
Qingfeng Chen: University of Texas Southwestern Medical Center
Changkeun Lee: University of Texas Southwestern Medical Center
Liping Chen: University of Texas Southwestern Medical Center
Yi Yang: University of Texas Southwestern Medical Center
Chunlei Cang: University of Pennsylvania
Dejian Ren: University of Pennsylvania
Youxing Jiang: University of Texas Southwestern Medical Center

Nature, 2016, vol. 531, issue 7593, 196-201

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature16446

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