ArticleThe Plant cell2001
The pore of plant K(+) channels is involved in voltage and pH sensing: domain-swapping between different K(+) channel alpha-subunits.
Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 43 citations in OpenAlex.
- Research Progress on Plant Shaker KPlants (Basel, Switzerland) · 2024Review
- External Cd2+ and protons activate the hyperpolarization-gated K+ channel KAT1 at the voltage sensor.The Journal of general physiology · 2021Article
- The Venus flytrap trigger hair-specific potassium channel KDM1 can reestablish the K+ gradient required for hapto-electric signaling.PLoS biology · 2020Article
- 14-3-3 Proteins in Guard Cell Signaling.Frontiers in plant science · 2015Review
- 30-year progress of membrane transport in plants.Planta · 2006Review
- Properties of shaker-type potassium channels in higher plants.The Journal of membrane biology · 2006Review
- A unique voltage sensor sensitizes the potassium channel AKT2 to phosphoregulation.The Journal of general physiology · 2005Article
- AKT2/3 subunits render guard cell K+ channels Ca2+ sensitive.The Journal of general physiology · 2005Article
- Histidines are responsible for zinc potentiation of the current in KDC1 carrot channels.Biophysical journal · 2004Article
- Outer pore residues control the H(+) and K(+) sensitivity of the Arabidopsis potassium channel AKT3.The Plant cell · 2002Article
- Channelling auxin action: modulation of ion transport by indole-3-acetic acid.Plant molecular biologyReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant K(+) uptake channel types differ with respect to their voltage, Ca(2)+, and pH dependence. Here, we constructed recombinant chimeric channels between KST1, a member of the inward-rectifying, acid-activated KAT1 family, and AKT3, a member of the weakly voltage-dependent, proton-blocked AKT2/3 family. The homologous pore regions of AKT3 (amino acids 216 to 287) and KST1 (amino acids 217 to 289) have been exchanged to generate the two chimeric channels AKT3/(p)KST1 and KST1/(p)AKT3. In contrast to AKT3 wild-type channels, AKT3/(p)KST1 revealed a strong inward rectification reminiscent of that of KST1. Correspondingly, the substitution of the KST1 by the AKT3 pore led to less pronounced rectification properties of KST1/(p)AKT3 compared with wild-type KST1. Besides the voltage dependence, the interaction between the chimera and extracellular H(+) and Ca(2)+ resembled the properties of the inserted rather than the respective wild-type pore. Whereas AKT3/(p)KST1 was acid activated and Ca(2)+ insensitive, extracellular protons and Ca(2)+ inhibited KST1/(p)AKT3. The regulation of the chimeric channels by cytoplasmic protons followed the respective wild-type backbone of the chimeric channels, indicating that the intracellular pH sensor is located outside the P domain. We thus conclude that essential elements for external pH and Ca(2)+ regulation and for the rectification of voltage-dependent K(+) uptake channels are located within the channel pore.
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