Evidence map›Paper›PMID 11432991›Full record

ArticleThe Journal of physiology2001

K(+)-dependent gating of K(ir)1.1 channels is linked to pH gating through a conformational change in the pore.

U Schulte, S Weidemann, J Ludwig, J Ruppersberg, B Fakler

Abstract read
In one paragraph

Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed.

  1. Article
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  4. Review
  5. Inhibition of ROMK channels by low extracellular K+ and oxidative stress.American journal of physiology. Renal physiology · 2013
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

U SchulteDepartment of Physiology II, University of Tübingen, Ob dem Himmelreich 7, 72074 Tübingen, Germany. uwe.schulte@uni-tuebingen.de
S Weidemann
J Ludwig
J Ruppersberg
B Fakler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. We have used giant patch-clamp recording to investigate the interaction between pH gating and K(+)-dependent gating in rat K(ir)1.1 (ROMK) channels heterologously expressed in Xenopus oocytes. 2. Gating by intracellular protons (pH gating) and extracellular K(+) ions (K(+)-dependent gating) is a hallmark of K(ir)1.1 channels that mediate K(+) secretion and control NaCl reabsorption in the kidney. pH gating is driven by protonation of an intracellular lysine residue (K80 in K(ir)1.1). K(+)-dependent gating occurs upon withdrawal of K(+) ions from the extracellular side of the channel. Both gating mechanisms are thought to interact allosterically. 3. K(+)-dependent gating was shown to be strictly coupled to pH gating; it only occurred when channels were in the pH-inactivated closed state, but not in the open state. Moreover, K(+)-dependent gating was absent in the non-pH-gated mutant K(ir)1.1(K80 M). 4. Channels inactivated by K(+)-dependent gating were reactivated upon addition of permeant ions to the extracellular side of the membrane, while impermeant ions failed to induce channel reactivation. Moreover, mutagenesis identified two residues in the P-helix (L136 and V140 in K(ir)1.1) that are crucial for K(+)-dependent gating. Replacement of these residues with the ones present in the non-K(+)-gated K(ir)2.1 abolished K(+)-dependent gating of K(ir)1.1 channels without affecting pH gating. 5. The results indicate that pH gating and K(+)-dependent gating are coupled to each other via structural rearrangements in the inner pore involving the P-helix.

Indexed as

Potassium Channels, Inwardly RectifyingAmino Acid SequenceAnimalsElectric ConductivityHydrogenHydrogen-Ion ConcentrationIon Channel GatingIonsModels, MolecularMolecular ConformationMolecular Sequence DataOocytesPatch-Clamp TechniquesPotassiumPotassium ChannelsXenopusHydrogenIonsKcnj1 protein, ratPotassiumPotassium ChannelsPotassium Channels, Inwardly Rectifying

Identifiers

PMID11432991
PMCPMC2278684

What OpenQuestion holds

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Registered trials

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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.