ArticleChannels (Austin, Tex.)
Kir4.1 K+ channels are regulated by external cations.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Astrocyte Kir4.1 expression level territorially controls excitatory transmission in the brain.Cell reports · 2025Article
- The physiological characteristics of inward rectifying potassium channel Kir4.2 and its research progress in human diseases.Frontiers in cell and developmental biology · 2025Review
- Non-trivial dynamics in a model of glial membrane voltage driven by open potassium pores.Biophysical journal · 2023Article
- Regulation of Papillary Muscle Contractility by NAD and Ammonia Interplay: Contribution of Ion Channels and Exchangers.Membranes · 2022Article
- A selectivity filter mutation provides insights into gating regulation of a KCommunications biology · 2022Article
- KGlia · 2021Article
- Aquaporin 4 as a NH3 Channel.The Journal of biological chemistry · 2016Article
- Cesium-associated hypokalemia successfully treated with amiloride.Clinical kidney journal · 2015Article
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- Inhibition of ROMK channels by low extracellular K+ and oxidative stress.American journal of physiology. Renal physiology · 2013Article
- Interactions of external K+ and internal blockers in a weak inward-rectifier K+ channel.The Journal of general physiology · 2012Article
- Residues at the outer mouth of Kir1.1 determine K-dependent gating.Biophysical journal · 2012Article
- Ion selectivity and current saturation in inward-rectifier K+ channels.The Journal of general physiology · 2012Article
- Potassium-dependent activation of Kir4.2 K⁺ channels.The Journal of physiology · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The inwardly rectifying potassium channel (Kir), Kir4.1 mediates spatial K(+)-buffering in the CNS. In this process the channel is potentially exposed to a large range of extracellular K(+) concentrations ([K(+)]o). We found that Kir4.1 is regulated by K(+)o. Increased [K(+)]o leads to a slow (mins) increase in the whole-cell currents of Xenopus oocytes expressing Kir4.1. Conversely, removing K(+) from the bath solution results in a slow decrease of the currents. This regulation is not coupled to the pHi-sensitive gate of the channel, nor does it require the presence of K67, a residue necessary for K(+)o-dependent regulation of Kir1.1. The voltage-dependent blockers Cs(+) and Ba(2+) substitute for K(+) and prevent deactivation of the channel in the absence of K(+)o. Cs(+) blocks and regulates the channel with similar affinity, consistent with the regulatory sites being in the selectivity-filter of the channel. Although both Rb(+) and NH4(+) permeate Kir4.1, only Rb(+) is able to regulate the channel. We conclude that Kir4.1 is regulated by ions interacting with specific sites in the selectivity filter. Using a kinetic model of the permeation process we show the plausibility of the channel's sensing the extracellular ionic environment through changes in the selectivity occupancy pattern, and that it is feasible for an ion with the selectivity properties of NH4(+) to permeate the channel without inducing these changes.
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