ArticleThe Journal of biological chemistry2012
Contribution of residues in second transmembrane domain of ASIC1a protein to ion selectivity.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.
- Ion Selectivity in the ENaC/DEG Family: A Systematic Review with Supporting Analysis.International journal of molecular sciences · 2021Pooled it
- Physiological insight into the conserved properties of Caenorhabditis elegans acid-sensing degenerin/epithelial sodium channels.The Journal of physiology · 2023Article
- A flexible GAS belt responds to pore mutations changing the ion selectivity of proton-gated channels.The Journal of general physiology · 2022Article
- Article
- Acid-sensing ion channels in sensory signaling.American journal of physiology. Renal physiology · 2020Review
- Evolutionarily Conserved Interactions within the Pore Domain of Acid-Sensing Ion Channels.Biophysical journal · 2020Article
- Determinants of ion selectivity in ASIC1a- and ASIC2a-containing acid-sensing ion channels.The Journal of general physiology · 2020Article
- Determinants of selective ion permeation in the epithelial NaThe Journal of general physiology · 2018Article
- Article
- Article
- Deactivation kinetics of acid-sensing ion channel 1a are strongly pH-sensitive.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Bile acids potentiate proton-activated currents inPhysiological reports · 2017Article
- Ion conduction and selectivity in acid-sensing ion channel 1.The Journal of general physiology · 2014Article
- Article
- Principles and properties of ion flow in P2X receptors.Frontiers in cellular neuroscience · 2014Review
- Independent contribution of extracellular proton binding sites to ASIC1a activation.The Journal of biological chemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Acid-sensing ion channels (ASICs) are proton-gated cation-selective channels expressed in the peripheral and central nervous systems. The ion permeation pathway of ASIC1a is defined by residues 426-450 in the second transmembrane (TM2) segment. The gate, formed by the intersection of the TM2 segments, localizes near the extracellular boundary of the plasma membrane. We explored the contribution to ion permeation and selectivity of residues in the TM2 segment of ASIC1a. Studies of accessibility with positively charged methanethiosulfonate reagents suggest that the permeation pathway in the open state constricts below the gate, restricting the passage to large ions. Substitution of residues in the intracellular vestibule at positions 437, 438, 443, or 446 significantly increased the permeability to K(+) versus Na(+). ASIC1a shows a selectivity sequence for alkali metals of Na(+)>Li(+)>K(+)≫Rb(+)>Cs(+). Alanine and cysteine substitutions at position 438 increased, to different extents, the relative permeability to Li(+), K(+), Rb(+), and Cs(+). For these mutants, ion permeation was not a function of the diameter of the nonhydrated ion, suggesting that Gly-438 encompasses an ion coordination site that is essential for ion selectivity. M437C and A443C mutants showed slightly increased permeability to K(+), Rb(+), and Cs(+), suggesting that substitutions at these positions influence ion discrimination by altering molecular sieving. Our results indicate that ion selectivity is accomplished by the contribution of multiple sites in the pore of ASIC1a.
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