Article,

TPC1 vacuole SV channel gains further shape - voltage priming of calcium-dependent gating

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Trends Plant Sci, 28 (6): 673-684 (2023)Hedrich, Rainer Muller, Thomas D Marten, Irene Becker, Dirk eng Research Support, Non-U.S. Gov't Review England 2023/02/06 Trends Plant Sci. 2023 Jun;28(6):673-684. doi: 10.1016/j.tplants.2023.01.001. Epub 2023 Feb 4..
DOI: 10.1016/j.tplants.2023.01.001

Abstract

Across phyla, voltage-gated ion channels (VGICs) allow excitability. The vacuolar two-pore channel AtTPC1 from the tiny mustard plant Arabidopsis thaliana has emerged as a paradigm for deciphering the role of voltage and calcium signals in membrane excitation. Among the numerous experimentally determined structures of VGICs, AtTPC1 was the first to be revealed in a closed and resting state, fueling speculation about structural rearrangements during channel activation. Two independent reports on the structure of a partially opened AtTPC1 channel protein have led to working models that offer promising insights into the molecular switches associated with the gating process. We review new structure-function models and also discuss the evolutionary impact of two-pore channels (TPCs) on K(+) homeostasis and vacuolar excitability.

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