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Plasticity of the selectivity filter is essential for permeation in lysosomal TPC2 channels.
Proc Natl Acad Sci U S A
August 2024
Department of Biochemistry, Structural Bioinformatics and Computational Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Two-pore channels are pathophysiologically important Na- and Ca-permeable channels expressed in lysosomes and other acidic organelles. Unlike most other ion channels, their permeability is malleable and ligand-tuned such that when gated by the signaling lipid PI(3,5)P, they are more Na-selective than when gated by the Ca mobilizing messenger nicotinic acid adenine dinucleotide phosphate. However, the structural basis that underlies such plasticity and single-channel behavior more generally remains poorly understood.
View Article and Find Full Text PDFTuning TPC2.
Cell Calcium
December 2022
The Calcium Signalling Group, Department of Biochemistry and Molecular Cell Biology, University Medical Center Hamburg-Eppendorf, Martinistrasse 52, Hamburg, 20246 Germany. Electronic address:
Tuning the ion selectivity of two-pore channels.
Proc Natl Acad Sci U S A
January 2017
Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9040;
Organellar two-pore channels (TPCs) contain two copies of a Shaker-like six-transmembrane (6-TM) domain in each subunit and are ubiquitously expressed in plants and animals. Interestingly, plant and animal TPCs share high sequence similarity in the filter region, yet exhibit drastically different ion selectivity. Plant TPC1 functions as a nonselective cation channel on the vacuole membrane, whereas mammalian TPC channels have been shown to be endo/lysosomal Na-selective or Ca-release channels.
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