ArticleThe Journal of general physiology2020
KV1.2 channels inactivate through a mechanism similar to C-type inactivation.
Article in The Journal of general physiology, 2020. 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, 19 citations in OpenAlex.
- Article
- Cryo-EM structures of Kv1.2 potassium channels, conducting and non-conducting.bioRxiv : the preprint server for biology · 2024Article
- Unmasking subtype-dependent susceptibility to C-type inactivation in mammalian Kv1 channels.Biophysical journal · 2024Article
- Sweetening K-channels: what sugar taught us about permeation and gating.Frontiers in molecular biosciences · 2023Review
- Kv1 channel inactivation: Slow and slower.The Journal of general physiology · 2022Article
- Mutations within the selectivity filter reveal that Kv1 channels have distinct propensities to slow inactivate.The Journal of general physiology · 2022Article
- Structural basis for C-type inactivation in a Shaker family voltage-gated KScience advances · 2022Article
- Structure of the Shaker Kv channel and mechanism of slow C-type inactivation.Science advances · 2022Article
- Shaker-IR K+ channel gating in heavy water: Role of structural water molecules in inactivation.The Journal of general physiology · 2021Article
- Exploring KFrontiers in molecular biosciences · 2021Article
- Tracking the motion of the KThe Journal of physiology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Slow inactivation has been described in multiple voltage-gated K+ channels and in great detail in the Drosophila Shaker channel. Structural studies have begun to facilitate a better understanding of the atomic details of this and other gating mechanisms. To date, the only voltage-gated potassium channels whose structure has been solved are KvAP (x-ray diffraction), the KV1.2-KV2.1 "paddle" chimera (x-ray diffraction and cryo-EM), KV1.2 (x-ray diffraction), and ether-à-go-go (cryo-EM); however, the structural details and mechanisms of slow inactivation in these channels are unknown or poorly characterized. Here, we present a detailed study of slow inactivation in the rat KV1.2 channel and show that it has some properties consistent with the C-type inactivation described in Shaker. We also study the effects of some mutations that are known to modulate C-type inactivation in Shaker and show that qualitative and quantitative differences exist in their functional effects, possibly underscoring subtle but important structural differences between the C-inactivated states in Shaker and KV1.2.
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