Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Handb Exp Pharmacol
2023 Jan 01;278:235-247. doi: 10.1007/164_2022_604.
Show Gene links
Show Anatomy links
The Plant Vacuole as Heterologous System to Characterize the Functional Properties of TPC Channels.
Dietrich P
,
Gradogna A
,
Carpaneto A
.
???displayArticle.abstract???
Human TPC channels are an emerging family of intracellular proteins fundamental for cell physiology and involved in various severe pathologies. Their localization in the membranes of endo-lysosomes, intracellular compartments of submicrometric dimensions, makes their study difficult with usual electrophysiological techniques. In this work, we show how the plant vacuole, a versatile organelle that can occupy up to 90% of the volume in mature plant cells, can be used as a heterologous system of expression for functional characterization. For this purpose, the use of vacuoles isolated from mesophyll cells of the Arabidopsis thaliana mutant lacking the endogenous TPC avoids unwanted interferences. The patch-clamp technique can be successfully applied to plant vacuoles in all different configuration modes; of note, the whole-vacuole configuration allows to study channel modulation by cytosolic factors. The combination of patch-clamp with fluorescence techniques, for example, by using fluorescent probes sensitive to specific ions of interest, represents a useful extension to investigate the selectivity properties of the channels. Therefore, the plant vacuole, similar to Xenopus oocytes for ion channels and transporters localized in the plasma membrane, has the capability to become a model system for functional studies on intracellular ion channels and transporters.
Benkerrou,
A perspective on the modulation of plant and animal two pore channels (TPCs) by the flavonoid naringenin.
2019, Pubmed
Benkerrou,
A perspective on the modulation of plant and animal two pore channels (TPCs) by the flavonoid naringenin.
2019,
Pubmed
Bertl,
Electrical measurements on endomembranes.
1992,
Pubmed
Boccaccio,
The phosphoinositide PI(3,5)P₂ mediates activation of mammalian but not plant TPC proteins: functional expression of endolysosomal channels in yeast and plant cells.
2014,
Pubmed
Brailoiu,
An NAADP-gated two-pore channel targeted to the plasma membrane uncouples triggering from amplifying Ca2+ signals.
2010,
Pubmed
Carpaneto,
Modulation of calcium and potassium permeation in plant TPC channels.
2018,
Pubmed
Carpaneto,
The phytotoxic lipodepsipeptide syringopeptin 25A from Pseudomonas syringae pv syringae forms ion channels in sugar beet vacuoles.
2002,
Pubmed
Carpaneto,
The signaling lipid phosphatidylinositol-3,5-bisphosphate targets plant CLC-a anion/H+ exchange activity.
2017,
Pubmed
Clementi,
Naringenin is a powerful inhibitor of SARS-CoV-2 infection in vitro.
2021,
Pubmed
Costa,
The Arabidopsis central vacuole as an expression system for intracellular transporters: functional characterization of the Cl-/H+ exchanger CLC-7.
2012,
Pubmed
,
Xenbase
Eisenach,
Plant vacuoles.
2015,
Pubmed
Favia,
VEGF-induced neoangiogenesis is mediated by NAADP and two-pore channel-2-dependent Ca2+ signaling.
2014,
Pubmed
Festa,
Using the plant vacuole as a biological system to investigate the functional properties of exogenous channels and transporters.
2016,
Pubmed
Filippini,
Could the Inhibition of Endo-Lysosomal Two-Pore Channels (TPCs) by the Natural Flavonoid Naringenin Represent an Option to Fight SARS-CoV-2 Infection?
2020,
Pubmed
Gradogna,
Fluorescence combined with excised patch: measuring calcium currents in plant cation channels.
2009,
Pubmed
Gradogna,
Beyond the patch-clamp resolution: functional activity of nonelectrogenic vacuolar NHX proton/potassium antiporters and inhibition by phosphoinositides.
2021,
Pubmed
Grimm,
Could an endo-lysosomal ion channel be the Achilles heel of SARS-CoV2?
2020,
Pubmed
Gunaratne,
Essential requirement for JPT2 in NAADP-evoked Ca2+ signaling.
2021,
Pubmed
Guo,
Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana.
2016,
Pubmed
Guo,
Tuning the ion selectivity of two-pore channels.
2017,
Pubmed
Hedrich,
Structure and Function of TPC1 Vacuole SV Channel Gains Shape.
2018,
Pubmed
Kintzer,
Structure, inhibition and regulation of two-pore channel TPC1 from Arabidopsis thaliana.
2016,
Pubmed
Kirsch,
Phosphatidylinositol-3,5-bisphosphate lipid-binding-induced activation of the human two-pore channel 2.
2018,
Pubmed
Lagostena,
The human two-pore channel 1 is modulated by cytosolic and luminal calcium.
2017,
Pubmed
Larisch,
The function of the two-pore channel TPC1 depends on dimerization of its carboxy-terminal helix.
2016,
Pubmed
Leisle,
ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1 for transport activity.
2011,
Pubmed
Martinoia,
Vacuolar Transporters - Companions on a Longtime Journey.
2018,
Pubmed
Milenkovic,
The mechanism and energetics of a ligand-controlled hydrophobic gate in a mammalian two pore channel.
2020,
Pubmed
Ou,
Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV.
2020,
Pubmed
Pafumi,
Naringenin Impairs Two-Pore Channel 2 Activity And Inhibits VEGF-Induced Angiogenesis.
2017,
Pubmed
Peiter,
The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement.
2005,
Pubmed
Pitt,
TPC2 is a novel NAADP-sensitive Ca2+ release channel, operating as a dual sensor of luminal pH and Ca2+.
2010,
Pubmed
She,
Structural mechanisms of phospholipid activation of the human TPC2 channel.
2019,
Pubmed
Stühmer,
Electrophysiologic recordings from Xenopus oocytes.
1998,
Pubmed
,
Xenbase
Tzfira,
pSAT vectors: a modular series of plasmids for autofluorescent protein tagging and expression of multiple genes in plants.
2005,
Pubmed
Wang,
TPC proteins are phosphoinositide- activated sodium-selective ion channels in endosomes and lysosomes.
2012,
Pubmed
Xu,
Lysosomal physiology.
2015,
Pubmed
Yoo,
Arabidopsis mesophyll protoplasts: a versatile cell system for transient gene expression analysis.
2007,
Pubmed
