ArticlePlant physiology2005
TPK1 is a vacuolar ion channel different from the slow-vacuolar cation channel.
Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 80 citations in OpenAlex.
- Characterization of human aquaporin ion channels in a yeast expression system as a tool for novel ion channel discovery.Bioscience reports · 2024Article
- A charged existence: A century of transmembrane ion transport in plants.Plant physiology · 2024Review
- Genomic analyses provide insights into the evolution and salinity adaptation of halophyte Tamarix chinensis.GigaScience · 2022Article
- New Insights into Plant TPK Ion Channel Evolution.Plants (Basel, Switzerland) · 2021Article
- Recent Advances in Genome-wide Analyses of Plant Potassium Transporter Families.Current genomics · 2021Review
- Transcriptomic Analysis of Salt-Stress-Responsive Genes in Barley Roots and Leaves.International journal of molecular sciences · 2021Article
- Potential Networks of Nitrogen-Phosphorus-Potassium Channels and Transporters in Arabidopsis Roots at a Single Cell Resolution.Frontiers in plant science · 2021Article
- Modulation of Ion Transport Across Plant Membranes by Polyamines: Understanding Specific Modes of Action Under Stress.Frontiers in plant science · 2020Article
- Review
- The Complex Fine-Tuning of K⁺ Fluxes in Plants in Relation to Osmotic and Ionic Abiotic Stresses.International journal of molecular sciences · 2019Review
- The Membrane Transport System of the Guard Cell and Its Integration for Stomatal Dynamics.Plant physiology · 2017Review
- Regulation of the Regulators: Post-Translational Modifications, Subcellular, and Spatiotemporal Distribution of Plant 14-3-3 Proteins.Frontiers in plant science · 2016Review
- K₂p channels in plants and animals.Pflugers Archiv : European journal of physiology · 2015Review
- 14-3-3 Proteins in Guard Cell Signaling.Frontiers in plant science · 2015Review
- Arabidopsis thaliana vacuolar TPK channels form functional K⁺ uptake pathways in Escherichia coli.Plant signaling & behavior · 2013Article
- Salt stress triggers phosphorylation of the Arabidopsis vacuolar K+ channel TPK1 by calcium-dependent protein kinases (CDPKs).Molecular plant · 2013Article
- The role of K(+) channels in uptake and redistribution of potassium in the model plant Arabidopsis thaliana.Frontiers in plant science · 2013Article
- Membrane localisation diversity of TPK channels and their physiological role.Plant signaling & behavior · 2011Article
- Rice two-pore K+ channels are expressed in different types of vacuoles.The Plant cell · 2011Article
- Calcium signals: the lead currency of plant information processing.The Plant cell · 2010Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TPK1 (formerly KCO1) is the founding member of the family of two-pore domain K(+) channels in Arabidopsis (Arabidopsis thaliana), which originally was described following expression in Sf9 insect cells as a Ca(2+)- and voltage-dependent outwardly rectifying plasma membrane K(+) channel. In plants, this channel has been shown by green fluorescent protein fusion to localize to the vacuolar membrane, which led to speculations that the TPK1 gene product would be a component of the nonselective, Ca(2+) and voltage-dependent slow-vacuolar (SV) cation channel found in many plants species. Using yeast (Saccharomyces cerevisiae) as an expression system for TPK1, we show functional expression of the channel in the vacuolar membrane. In isolated vacuoles of yeast yvc1 disruption mutants, the TPK1 gene product shows ion channel activity with some characteristics very similar to the SV-type channel. The open channel conductance of TPK1 in symmetrically 100 mM KCl is slightly asymmetric with roughly 40 pS at positive membrane voltages and 75 pS at negative voltages. Similar to the SV-type channel, TPK1 is activated by cytosolic Ca(2+), requiring micromolar concentration for activation. However, in contrast to the SV-type channel, TPK1 exhibits strong selectivity for K(+) over Na(+), and its activity turned out to be independent of the membrane voltage over the range of +/-80 mV. Our data clearly demonstrate that TPK1 is a voltage-independent, Ca(2+)-activated, K(+)-selective ion channel in the vacuolar membrane that does not mediate SV-type ionic currents.
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