Article,

Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels

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Elife, (2023)Lu, Jinping Dreyer, Ingo Dickinson, Miles Sasha Panzer, Sabine Jaslan, Dawid Navarro-Retamal, Carlos Geiger, Dietmar Terpitz, Ulrich Becker, Dirk Stroud, Robert M Marten, Irene Hedrich, Rainer eng Koselleck award HE 1640/42-1/Deutsche Forschungsgemeinschaft/ priority programs 'MAdLand - Molecular Adaptation to Land: Plant Evolution to Change' HE 1640/45-1/Deutsche Forschungsgemeinschaft/ priority programs 'MAdLand - Molecular Adaptation to Land: Plant Evolution to Change' BE1867/9-1/Deutsche Forschungsgemeinschaft/ doctoral fellowship/China Scholarship Council/ STIPET fellowship/Deutscher Akademischer Austauschdienst/ FONDEQUIP EQM160063/Comision Nacional de Investigacion Cientifica y Tecnologica/ ATE220043/Anilio-Anid/ 3170434/Fondo Nacional de Desarrollo Cientifico y Tecnologico/ 1220504/Fondo Nacional de Desarrollo Cientifico y Tecnologico/ England 2023/11/22 Elife. 2023 Nov 22;12:e86384. doi: 10.7554/eLife.86384..
DOI: 10.7554/eLife.86384

Abstract

To fire action-potential-like electrical signals, the vacuole membrane requires the two-pore channel TPC1, formerly called SV channel. The TPC1/SV channel functions as a depolarization-stimulated, non-selective cation channel that is inhibited by luminal Ca(2+). In our search for species-dependent functional TPC1 channel variants with different luminal Ca(2+) sensitivity, we found in total three acidic residues present in Ca(2+) sensor sites 2 and 3 of the Ca(2+)-sensitive AtTPC1 channel from Arabidopsis thaliana that were neutral in its Vicia faba ortholog and also in those of many other Fabaceae. When expressed in the Arabidopsis AtTPC1-loss-of-function background, wild-type VfTPC1 was hypersensitive to vacuole depolarization and only weakly sensitive to blocking luminal Ca(2+). When AtTPC1 was mutated for these VfTPC1-homologous polymorphic residues, two neutral substitutions in Ca(2+) sensor site 3 alone were already sufficient for the Arabidopsis At-VfTPC1 channel mutant to gain VfTPC1-like voltage and luminal Ca(2+) sensitivity that together rendered vacuoles hyperexcitable. Thus, natural TPC1 channel variants exist in plant families which may fine-tune vacuole excitability and adapt it to environmental settings of the particular ecological niche.

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