ArticleBiophysical journal2004
The external TEA binding site and C-type inactivation in voltage-gated potassium channels.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Article
- Article
- Mechanism of use-dependent Kv2 channel inhibition by RY785.The Journal of general physiology · 2022Article
- GFP-Margatoxin, a Genetically Encoded Fluorescent Ligand to Probe Affinity of Kv1.3 Channel Blockers.International journal of molecular sciences · 2022Article
- Antispasmodic Effect of Asperidine B, a Pyrrolidine Derivative, through Inhibition of L-Type CaMolecules (Basel, Switzerland) · 2021Article
- KV1.2 channels inactivate through a mechanism similar to C-type inactivation.The Journal of general physiology · 2020Article
- Variability of Potassium Channel Blockers in Mesobuthus eupeus Scorpion Venom with Focus on Kv1.1: AN INTEGRATED TRANSCRIPTOMIC AND PROTEOMIC STUDY.The Journal of biological chemistry · 2015Article
- Mechanism of Cd2+ coordination during slow inactivation in potassium channels.Structure (London, England : 1993) · 2012Article
- Tuning the tetraethylammonium sensitivity of potassium channel Kcv by subunit combination.The Journal of general physiology · 2012Article
- Arrangement of Kv1 alpha subunits dictates sensitivity to tetraethylammonium.The Journal of general physiology · 2010Article
- Dependence of 6beta-acetoxy-7alpha-hydroxyroyleanone block of Kv1.2 channels on C-type inactivation.Cellular and molecular life sciences : CMLS · 2010Article
- The binding of donepezil with external mouth of K+-channels of molluscan neurons.Cellular and molecular neurobiology · 2009Article
- External Ba2+ block of human Kv1.5 at neutral and acidic pH: evidence for Ho+-induced constriction of the outer pore mouth at rest.Biophysical journal · 2008Article
- Blocker protection by short spermine analogs: refined mapping of the spermine binding site in a Kir channel.Biophysical journal · 2008Article
- Voltage-dependent C-type inactivation in a constitutively open K+ channel.Biophysical journal · 2008Article
- Effects of changes in extracellular pH and potassium concentration on Kv1.3 inactivation.European biophysics journal : EBJ · 2008Article
- Modification of K+ channel-drug interactions by ancillary subunits.The Journal of physiology · 2008Review
- A cation-pi interaction between extracellular TEA and an aromatic residue in potassium channels.The Journal of general physiology · 2006Article
- Pharmacology and surface electrostatics of the K channel outer pore vestibule.The Journal of membrane biology · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The location of the tetraethylammonium (TEA) binding site in the outer vestibule of K+ channels, and the mechanism by which external TEA slows C-type inactivation, have been considered well-understood. The prevailing model has been that TEA is coordinated by four amino acid side chains at the position equivalent to Shaker T449, and that TEA prevents a constriction that underlies inactivation via a foot-in-the-door mechanism at this same position. However, a growing body of evidence has suggested that this picture may not be entirely correct. In this study, we reexamined these two issues, using both the Kv2.1 and Shaker potassium channels. In contrast to results previously obtained with Shaker, substitution of the tyrosine at Kv2.1 position 380 (equivalent to Shaker 449) with a threonine or cysteine had a relatively minor effect on TEA potency. In both Kv2.1 and Shaker, modification of cysteines at position 380/449 by 2-(trimethylammonium)ethyl methanethiosulfonate (MTSET) proceeded at identical rates in the absence and presence of TEA. Additional experiments in Shaker demonstrated that TEA bound well to C-type inactivated channels, but did not interfere with MTSET modification of C449 in inactivated channels. Together, these findings rule out the possibility that TEA binding involves an intimate interaction with the four side chains at the position equivalent to Shaker 449. Moreover, these results argue against the model whereby TEA slows inactivation via a foot-in-the-door mechanism at position 449, and also argue against the hypothesis that the position 449 side chains move toward the center of the conduction pathway during inactivation. Occupancy by TEA completely prevented MTSET modification of a cysteine in the outer-vestibule turret (Kv2.1 position 356/Shaker position 425), which has been shown to interfere with both TEA binding and the interaction of K+ with an external binding site. Together, these data suggest that TEA is stabilized in a more external position in the outer vestibule, and does not bind via direct coordination with any specific outer-vestibule residues.
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