Evidence map›Paper›PMID 12829485›Full record

ArticleBiophysical journal2003

The pore helix is involved in stabilizing the open state of inwardly rectifying K+ channels.

Noga Alagem, Semen Yesylevskyy, Eitan Reuveny

Abstract readComparative Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
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  17. Uncoupling proton activation of vanilloid receptor TRPV1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  18. Article
  19. Article
  20. Evolving potassium channels by means of yeast selection reveals structural elements important for selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
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

3 authors.

Noga AlagemDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Semen Yesylevskyy
Eitan Reuveny

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ion channels can be gated by various extrinsic cues, such as voltage, pH, and second messengers. However, most ion channels display extrinsic cue-independent transitions as well. These events represent spontaneous conformational changes of the channel protein. The molecular basis for spontaneous gating and its relation to the mechanism by which channels undergo activation gating by extrinsic cue stimulation is not well understood. Here we show that the proximal pore helix of inwardly rectifying (Kir) channels is partially responsible for determining spontaneous gating characteristics, affecting the open state of the channel by stabilizing intraburst openings as well as the bursting state itself without affecting K(+) ion-channel interactions. The effect of the pore helix on the open state of the channel is qualitatively similar to that of two well-characterized mutations at the second transmembrane domain (TM2), which stabilize the channel in its activated state. However, the effects of the pore helix and the TM2 mutations on gating were additive and independent of each other. Moreover, in sharp contrast to the two TM2 mutations, the pore helix mutation did not affect the functionality of the agonist-responsive gate. Our results suggest that in Kir channels, the bottom of the pore helix and agonist-induced conformational transitions at the TM2 ultimately stabilize via different pathways the open conformation of the same gate.

Indexed as

AnimalsG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIon Channel GatingMembrane PotentialsMutationOocytesPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein ConformationProtein Structure, TertiaryProtein SubunitsRecombinant ProteinsStructure-Activity RelationshipXenopus laevisG Protein-Coupled Inwardly-Rectifying Potassium ChannelsKCNJ5 protein, humanPotassiumPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein SubunitsRecombinant Proteins

Identifiers

PMID12829485
PMCPMC1303086

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.