ArticleProceedings of the National Academy of Sciences of the United States of America1999
Channel-mediated high-affinity K+ uptake into guard cells from Arabidopsis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- The Venus flytrap trigger hair-specific potassium channel KDM1 can reestablish the K+ gradient required for hapto-electric signaling.PLoS biology · 2020Article
- Unique features of the grapevine VvK5.1 channel support novel functions for outward K+ channels in plants.Journal of experimental botany · 2019Article
- Calcium sensor kinase activates potassium uptake systems in gland cells of Venus flytraps.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Dysregulation of ion homeostasis by antifungal agents.Frontiers in microbiology · 2012Article
- Heteromeric AtKC1{middle dot}AKT1 channels in Arabidopsis roots facilitate growth under K+-limiting conditions.The Journal of biological chemistry · 2009Article
- Emergence of a novel calcium signaling pathway in plants: CBL-CIPK signaling network.Physiology and molecular biology of plants : an international journal of functional plant biology · 2008Article
- 30-year progress of membrane transport in plants.Planta · 2006Review
- AKT2/3 subunits render guard cell K+ channels Ca2+ sensitive.The Journal of general physiology · 2005Article
- Regulation by external K+ in a maize inward shaker channel targets transport activity in the high concentration range.The Plant cell · 2005Article
- Outer pore residues control the H(+) and K(+) sensitivity of the Arabidopsis potassium channel AKT3.The Plant cell · 2002Article
- Extracellular protons inhibit the activity of inward-rectifying potassium channels in the motor cells of Samanea saman pulvini.Plant physiology · 2001Article
- KAT1 is not essential for stomatal opening.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Expression and stress-dependent induction of potassium channel transcripts in the common ice plant.Plant physiology · 2001Article
- Mutation in pore domain uncovers cation- and voltage-sensitive recovery from inactivation in KAT1 channel.Biophysical journal · 2000Article
- Histidine(118) in the S2-S3 linker specifically controls activation of the KAT1 channel expressed in Xenopus oocytes.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potassium uptake by higher plants is the result of high- or low-affinity transport accomplished by different sets of transporters. Although K+ channels were thought to mediate low-affinity uptake only, the molecular mechanism of the high-affinity, proton-dependent K+ uptake system is still scant. Taking advantage of the high-current resolution of the patch-clamp technique when applied to the small Arabidopsis thaliana guard cells densely packed with voltage-dependent K+ channels, we could directly record channels working in the concentration range of high-affinity K+ uptake systems. Here we show that the K+ channel KAT1 expressed in Arabidopsis guard cells and yeast is capable of mediating potassium uptake from media containing as little as 10 microM of external K+. Upon reduction of the external K+ content to the micromolar level the voltage dependence of the channel remained unaffected, indicating that this channel type represents a voltage sensor rather than a K+-sensing valve. This behavior results in K+ release through K+ uptake channels whenever the Nernst potential is negative to the activation threshold of the channel. In contrast to the H+-coupled K+ symport shown to account for high-affinity K+ uptake in roots, pH-dependent K+ uptake into guard cells is a result of a shift in the voltage dependence of the K+ channel. We conclude that plant K+ channels activated by acid pH may play an essential role in K+ uptake even from dilute solutions.
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