ArticlePLoS biology2008
The desensitization gating of the MthK K+ channel is governed by its cytoplasmic amino terminus.
Article in PLoS biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Lipid trapping slows ball-and-chain inactivation in a calcium-activated potassium channel.Nature communications · 2026Article
- Resurgent current in context: Insights from the structure and function of Na and K channels.Biophysical journal · 2024Review
- N-type fast inactivation of a eukaryotic voltage-gated sodium channel.Nature communications · 2022Article
- Molecular Mechanisms for Bacterial Potassium Homeostasis.Journal of molecular biology · 2021Review
- Article
- Polyamine blockade and binding energetics in the MthK potassium channel.The Journal of general physiology · 2020Article
- Article
- Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling.Nature communications · 2019Article
- Calcium ions open a selectivity filter gate during activation of the MthK potassium channel.Nature communications · 2015Article
- Structure of the MthK RCK in complex with cadmium.Journal of structural biology · 2010Article
- KTN (RCK) domains regulate K+ channels and transporters by controlling the dimer-hinge conformation.Structure (London, England : 1993) · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The RCK-containing MthK channel undergoes two inactivation processes: activation-coupled desensitization and acid-induced inactivation. The acid inactivation is mediated by the C-terminal RCK domain assembly. Here, we report that the desensitization gating is governed by a desensitization domain (DD) of the cytoplasmic N-terminal 17 residues. Deletion of DD completely removes the desensitization, and the process can be fully restored by a synthetic DD peptide added in trans. Mutagenesis analyses reveal a sequence-specific determinant for desensitization within the initial hydrophobic segment of DD. Proton nuclear magnetic resonance ((1)H NMR) spectroscopy analyses with synthetic peptides and isolated RCK show interactions between the two terminal domains. Additionally, we show that deletion of DD does not affect the acid-induced inactivation, indicating that the two inactivation processes are mutually independent. Our results demonstrate that the short N-terminal DD of MthK functions as a complete moveable module responsible for the desensitization. Its interaction with the C-terminal RCK domain may play a role in the gating process.
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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.