ArticleThe Journal of general physiology2006
The polyamine binding site in inward rectifier K+ channels.
Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 85 citations in OpenAlex.
- Cryo-EM structures of heteromeric Kir4.1/5.1 channel suggest mechanisms of inward rectification and channel blockage.Nature communications · 2026Article
- Biogenic Amine Metabolism and Its Genetic Variations in Autism Spectrum Disorder: A Comprehensive Overview.Biomolecules · 2025Review
- The role of polyamine metabolism in cellular function and physiology.American journal of physiology. Cell physiology · 2024Review
- Recent Advances in Fluorescent Methods for Polyamine Detection and the Polyamine Suppressing Strategy in Tumor Treatment.Biosensors · 2022Review
- Polyamine Immunometabolism: Central Regulators of Inflammation, Cancer and Autoimmunity.Cells · 2022Review
- Simulating PIPFrontiers in molecular biosciences · 2021Article
- Diamine Biosynthesis: Research Progress and Application Prospects.Applied and environmental microbiology · 2020Review
- Polyamine blockade and binding energetics in the MthK potassium channel.The Journal of general physiology · 2020Article
- Polyamines and potassium channels: A 25-year romance.The Journal of biological chemistry · 2018Review
- Bioelectrical control of positional information in development and regeneration: A review of conceptual and computational advances.Progress in biophysics and molecular biology · 2018Review
- Expression, purification, and electrophysiological characterization of a recombinant, fluorescent Kir6.2 in mammalian cells.Protein expression and purification · 2018Article
- New Insights Into Permeation of Large Cations Through ATP-Gated P2X Receptors.Frontiers in molecular neuroscience · 2018Article
- Bioelectric gene and reaction networks: computational modelling of genetic, biochemical and bioelectrical dynamics in pattern regulation.Journal of the Royal Society, Interface · 2017Article
- Elucidating the Structure ofACS omega · 2017Article
- Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.The Journal of biological chemistry · 2017Article
- Apigenin Inhibits Human SW620 Cell Growth by Targeting Polyamine Catabolism.Evidence-based complementary and alternative medicine : eCAM · 2017Article
- Mechanism for attenuated outward conductance induced by mutations in the cytoplasmic pore of Kir2.1 channels.Scientific reports · 2015Article
- Akt and Erk1/2 activate the ornithine decarboxylase/polyamine system in cardioprotective ischemic preconditioning in rats: the role of mitochondrial permeability transition pores.Molecular and cellular biochemistry · 2014Article
- Polyamine catabolism in carcinogenesis: potential targets for chemotherapy and chemoprevention.Amino acids · 2014Review
- 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
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Strongly inwardly rectifying potassium channels exhibit potent and steeply voltage-dependent block by intracellular polyamines. To locate the polyamine binding site, we have examined the effects of polyamine blockade on the rate of MTSEA modification of cysteine residues strategically substituted in the pore of a strongly rectifying Kir channel (Kir6.2[N160D]). Spermine only protected cysteines substituted at a deep location in the pore, between the "rectification controller" residue (N160D in Kir6.2, D172 in Kir2.1) and the selectivity filter, against MTSEA modification. In contrast, blockade with a longer synthetic polyamine (CGC-11179) also protected cysteines substituted at sites closer to the cytoplasmic entrance of the channel. Modification of a cysteine at the entrance to the inner cavity (169C) was unaffected by either spermine or CGC-11179, and spermine was clearly "locked" into the inner cavity (i.e., exhibited a dramatically slower exit rate) following modification of this residue. These data provide physical constraints on the spermine binding site, demonstrating that spermine stably binds at a deep site beyond the "rectification controller" residue, near the extracellular entrance to the channel.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.