ArticleThe Journal of general physiology2004
Molecular basis of inward rectification: polyamine interaction sites located by combined channel and ligand mutagenesis.
Article in The Journal of general physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Atomistic mechanisms of calcium permeation modulated by Q/R editing and selectivity filter mutations in GluA2 AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A phenylalanine at the extracellular side of Kir1.1 facilitates potassium permeation.Channels (Austin, Tex.) · 2024Article
- Subunit gating resulting from individual protonation events in Kir2 channels.Nature communications · 2023Article
- Subunit gating resulting from individual protonation events in Kir2 channels.Research square · 2023Article
- Chronic Propafenone Application Increases Functional KPharmaceuticals (Basel, Switzerland) · 2023Article
- Seeing spermine blocking of K+ ion movement through inward rectifier Kir2.2 channels.The Journal of general physiology · 2023Article
- Simulating PIPFrontiers in molecular biosciences · 2021Article
- Polyamine blockade and binding energetics in the MthK potassium channel.The Journal of general physiology · 2020Article
- Computational Insights Into Voltage Dependence of Polyamine Block in a Strong Inwardly Rectifying KFrontiers in pharmacology · 2020Article
- A small viral potassium ion channel with an inherent inward rectification.Channels (Austin, Tex.) · 2019Article
- Extracellular Spermine Triggers a Rapid Intracellular Phosphatidic Acid Response in Arabidopsis, Involving PLDδ Activation and Stimulating Ion Flux.Frontiers in plant science · 2019Article
- Polyamines and potassium channels: A 25-year romance.The Journal of biological chemistry · 2018Review
- A synergistic blocking effect of Mg²⁺ and spermine on the inward rectifier K⁺ (Kir2.1) channel pore.Scientific reports · 2016Article
- Role of a Hydrophobic Pocket in Polyamine Interactions with the Polyspecific Organic Cation Transporter OCT3.The Journal of biological chemistry · 2015Article
- The bundle crossing region is responsible for the inwardly rectifying internal spermine block of the Kir2.1 channel.Pflugers Archiv : European journal of physiology · 2014Article
- Inward rectifiers and their regulation by endogenous polyamines.Frontiers in physiology · 2014Review
- Scanning the topography of polyamine blocker binding in an inwardly rectifying potassium channel.The Journal of biological chemistry · 2013Article
- Molecular mechanisms of chloroquine inhibition of heterologously expressed Kir6.2/SUR2A channels.Molecular pharmacology · 2012Article
- Multi-ion distributions in the cytoplasmic domain of inward rectifier potassium channels.Biophysical journal · 2012Article
- Integrin α9β1 in airway smooth muscle suppresses exaggerated airway narrowing.The Journal of clinical investigation · 2012Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Polyamines cause inward rectification of (Kir) K+ channels, but the mechanism is controversial. We employed scanning mutagenesis of Kir6.2, and a structural series of blocking diamines, to combinatorially examine the role of both channel and blocker charges. We find that introduced glutamates at any pore-facing residue in the inner cavity, up to and including the entrance to the selectivity filter, can confer strong rectification. As these negative charges are moved higher (toward the selectivity filter), or lower (toward the cytoplasm), they preferentially enhance the potency of block by shorter, or longer, diamines, respectively. MTSEA+ modification of engineered cysteines in the inner cavity reduces rectification, but modification below the inner cavity slows spermine entry and exit, without changing steady-state rectification. The data provide a coherent explanation of classical strong rectification as the result of polyamine block in the inner cavity and selectivity filter.
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