%0 Journal Article %1 lu2023vicia %A Lu, Jinping %A Dreyer, Ingo %A Dickinson, Miles Sasha %A Panzer, Sabine %A Jaślan, Dawid %A Navarro-Retamal, Carlos %A Geiger, Dietmar %A Terpitz, Ulrich %A Becker, Dirk %A Stroud, Robert M %A Marten, Irene %A Hedrich, Rainer %C England %D 2023 %J eLife %K imported %P e86384-- %R 10.7554/eLife.86384 %T Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels %U https://pubmed.ncbi.nlm.nih.gov/37991833 %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 = {2024-02-16T11:44:22.000+0100}, address = {England}, author = {Lu, Jinping and Dreyer, Ingo and Dickinson, Miles Sasha and Panzer, Sabine and Jaślan, Dawid and Navarro-Retamal, Carlos and Geiger, Dietmar and Terpitz, Ulrich and Becker, Dirk and Stroud, Robert M and Marten, Irene and Hedrich, Rainer}, biburl = {https://www.bibsonomy.org/bibtex/26e82f453929761b63bdfb59838f4b000/imarten}, comment = {37991833[pmid] PMC10665017[pmcid]}, description = {Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels - PubMed}, doi = {10.7554/eLife.86384}, interhash = {62597503810c1dee01c7010b917a0d6a}, intrahash = {6e82f453929761b63bdfb59838f4b000}, issn = {2050084X}, journal = {eLife}, keywords = {imported}, month = nov, pages = {e86384--}, timestamp = {2024-02-16T11:44:22.000+0100}, title = {Vicia faba SV channel VfTPC1 is a hyperexcitable variant of plant vacuole Two Pore Channels}, url = {https://pubmed.ncbi.nlm.nih.gov/37991833}, volume = 12, year = 2023 }