ArticlePflugers Archiv : European journal of physiology2015
Interactions between the N-terminal tail and the gating machinery of hERG K⁺ channels both in closed and open/inactive states.
Article in Pflugers Archiv : European journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The EAG Voltage-Dependent KFrontiers in pharmacology · 2020Review
- Modulation of hERG KFrontiers in pharmacology · 2020Review
- Extracellular protons accelerate hERG channel deactivation by destabilizing voltage sensor relaxation.The Journal of general physiology · 2019Article
- New Structures and Gating of Voltage-Dependent Potassium (Kv) Channels and Their Relatives: A Multi-Domain and Dynamic Question.International journal of molecular sciences · 2019Review
- Relative positioning of Kv11.1 (hERG) KScientific reports · 2018Article
- Functional characterization of Kv11.1 (hERG) potassium channels split in the voltage-sensing domain.Pflugers Archiv : European journal of physiology · 2018Article
- Gating mechanism of Kv11.1 (hERG) KPflugers Archiv : European journal of physiology · 2018Article
- Multifunctional ion transport properties of human SLC4A11: comparison of the SLC4A11-B and SLC4A11-C variants.American journal of physiology. Cell physiology · 2016Article
- Bimodal regulation of an Elk subfamily K+ channel by phosphatidylinositol 4,5-bisphosphate.The Journal of general physiology · 2015Article
- Conservation analysis of residues in the S4-S5 linker and the terminal part of the S5-P-S6 pore modulus in Kv and HCN channels: flexible determinants for the electromechanical coupling.Pflugers Archiv : European journal of physiology · 2015Article
- An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome.Human mutation · 2015Article
- C-Linker Accounts for Differential Sensitivity of ERG1 and ERG2 K+ Channels to RPR260243-Induced Slow Deactivation.Molecular pharmacology · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal-most N-tail of the human ether-à-go-go-related gene (hERG) potassium channel is a crucial modulator of deactivation through its interactions with the S4-S5 loop and/or the C-linker/cNBD, leading to a stabilization of the channel's open state. Not only the N-terminal, but also the initial C-terminal region of the channel can modulate the transitions between the open and closed states either by direct or by indirect/allosteric interactions with the gating machinery. However, while a physical proximity of the N-tail to the gating machinery has been demonstrated in the closed state, data about their possible interaction in other channel conformations have been lacking. Using a site-directed cysteine mutagenesis and disulfide chemistry approach, we present here evidence that a physical proximity between the N-tail and the gating-related structures can also exist in channels held between pulses in the open/inactive state, highlighting the physiological and functional relevance of the direct interactions between the N-terminal tail and the S4-S5 loop and/or C-linker structures for modulation of channel.
Indexed as
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Registered trials
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