Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels
J. Lu, I. Dreyer, M. Dickinson, S. Panzer, D. Jaslan, C. Navarro-Retamal, D. Geiger, U. Terpitz, D. Becker, R. Stroud, I. Marten, and R. Hedrich. 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.
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.
%0 Journal Article
%1 lu2023vicia
%A Lu, J.
%A Dreyer, I.
%A Dickinson, M. S.
%A Panzer, S.
%A Jaslan, D.
%A Navarro-Retamal, C.
%A Geiger, D.
%A Terpitz, U.
%A Becker, D.
%A Stroud, R. M.
%A Marten, I.
%A Hedrich, R.
%D 2023
%J Elife
%K Vacuoles myOwn uni_network
%R 10.7554/eLife.86384
%T Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels
%U https://www.ncbi.nlm.nih.gov/pubmed/37991833https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10665017/pdf/elife-86384.pdf
%V 12
%X 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.
@article{lu2023vicia,
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.},
added-at = {2024-02-15T15:11:54.000+0100},
author = {Lu, J. and Dreyer, I. and Dickinson, M. S. and Panzer, S. and Jaslan, D. and Navarro-Retamal, C. and Geiger, D. and Terpitz, U. and Becker, D. and Stroud, R. M. and Marten, I. and Hedrich, R.},
biburl = {https://www.bibsonomy.org/bibtex/2854c0ae164d8c16afdee72a790de75aa/jvsi_all},
doi = {10.7554/eLife.86384},
interhash = {03d60e6c02ca0cffc6f1166c14b35d73},
intrahash = {854c0ae164d8c16afdee72a790de75aa},
issn = {2050-084X (Electronic)
2050-084X (Linking)},
journal = {Elife},
keywords = {Vacuoles myOwn uni_network},
note = {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.},
timestamp = {2024-02-15T15:11:54.000+0100},
title = {Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels},
type = {Journal Article},
url = {https://www.ncbi.nlm.nih.gov/pubmed/37991833https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10665017/pdf/elife-86384.pdf},
volume = 12,
year = 2023
}