ArticlePlant physiology2003
Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel.
Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Article
- Genome-wide identification, characterization and expression analysis of CNGC Genes in moso bamboo (Phyllostachys edulis).BMC plant biology · 2025Article
- Cryo-EM structures of Arabidopsis CNGC1 and CNGC5 reveal molecular mechanisms underlying gating and calcium selectivity.Nature plants · 2025Article
- Analysis ofInternational journal of molecular sciences · 2025Article
- Effects of Potassium-Containing Fertilizers on Sugar and Organic Acid Metabolism in Grape Fruits.International journal of molecular sciences · 2024Article
- A salt stress-activated GSO1-SOS2-SOS1 module protects the Arabidopsis root stem cell niche by enhancing sodium ion extrusion.The EMBO journal · 2023Article
- Delineating Calcium Signaling Machinery in Plants: Tapping the Potential through Functional Genomics.Current genomics · 2021Review
- The Complex Story of Plant Cyclic Nucleotide-Gated Channels.International journal of molecular sciences · 2021Review
- Potential Networks of Nitrogen-Phosphorus-Potassium Channels and Transporters in Arabidopsis Roots at a Single Cell Resolution.Frontiers in plant science · 2021Article
- Plant Cyclic Nucleotide-Gated Channels: New Insights on Their Functions and Regulation.Plant physiology · 2020Article
- MgInternational journal of molecular sciences · 2020Article
- Plant Membrane Transport Research in the Post-genomic Era.Plant communications · 2020Review
- Evolution and Structural Characteristics of Plant Voltage-Gated KThe Plant cell · 2018Review
- Short day length-induced decrease of cesium uptake without altering potassium uptake manner in poplar.Scientific reports · 2016Article
- The arabidopsis cyclic nucleotide interactome.Cell communication and signaling : CCS · 2016Article
- A Guide to Transient Expression of Membrane Proteins in HEK-293 Cells for Functional Characterization.Frontiers in physiology · 2016Article
- Phytosulfokine Regulates Growth in Arabidopsis through a Response Module at the Plasma Membrane That Includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1.The Plant cell · 2015Article
- Plant salt-tolerance mechanisms.Trends in plant science · 2014Review
- Cyclic nucleotide gated channels 7 and 8 are essential for male reproductive fertility.PloS one · 2013Article
- Plant organellar calcium signalling: an emerging field.Journal of experimental botany · 2012Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding of the molecular architecture necessary for selective K(+) permeation through the pore of ion channels is based primarily on analysis of the crystal structure of the bacterial K(+) channel KcsA, and structure:function studies of cloned animal K(+) channels. Little is known about the conduction properties of a large family of plant proteins with structural similarities to cloned animal cyclic nucleotide-gated channels (CNGCs). Animal CNGCs are nonselective cation channels that do not discriminate between Na(+) and K(+) permeation. These channels all have the same triplet of amino acids in the channel pore ion selectivity filter, and this sequence is different from that of the selectivity filter found in K(+)-selective channels. Plant CNGCs have unique pore selectivity filters; unlike those found in any other family of channels. At present, the significance of the unique pore selectivity filters of plant CNGCs, with regard to discrimination between Na(+) and K(+) permeation is unresolved. Here, we present an electrophysiological analysis of several members of this protein family; identifying the first cloned plant channel (AtCNGC1) that conducts Na(+). Another member of this ion channel family (AtCNGC2) is shown to have a selectivity filter that provides a heretofore unknown molecular basis for discrimination between K(+) and Na(+) permeation. Specific amino acids within the AtCNGC2 pore selectivity filter (Asn-416, Asp-417) are demonstrated to facilitate K(+) over Na(+) conductance. The selectivity filter of AtCNGC2 represents an alternative mechanism to the well-known GYG amino acid triplet of K(+) channels that has been identified as the critical basis for K(+) over Na(+) permeation through the pore of ion channels.
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