Evidence map›Paper›PMID 12770878›Full record

ArticleBiophysical journal2003

Contribution of cytosolic cysteine residues to the gating properties of the Kir2.1 inward rectifier.

L Garneau, H Klein, L Parent, R Sauvé

Open access · bronzeAbstract read
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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 44% of its field
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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Redox Regulation of KAntioxidants & redox signaling · 2024
    Review
  2. Extracellular Kir2.1Circulation research · 2024
    Article
  3. Extracellular cysteine disulfide bond break at Cys122 disrupts PIPbioRxiv : the preprint server for biology · 2023
    Article
  4. Chronic Propafenone Application Increases Functional KPharmaceuticals (Basel, Switzerland) · 2023
    Article
  5. From Crosstalk to Synergism: The Combined Effect of Cholesterol and PI(4,5)PAdvances in experimental medicine and biology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Flecainide increases Kir2.1 currents by interacting with cysteine 311, decreasing the polyamine-induced rectification.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Article
  11. Article
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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

4 authors at 1 institution in 1 country.

L GarneauDépartement de physiologie, Groupe de recherche en transport membranaire, Faculté de médecine, Université de Montréal, Montréal, Québec, Canada H3C 3J7.
H Klein
L Parent
R Sauvé
Université de Montréal · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The topological model proposed for the Kir2.1 inward rectifier predicts that seven of the channel 13 cysteine residues are distributed along the N- and C-terminus regions, with some of the residues comprised within highly conserved domains involved in channel gating. To determine if cytosolic cysteine residues contribute to the gating properties of Kir2.1, each of the N- and C-terminus cysteines was mutated into either a polar (S, D, N), an aliphatic (A,V, L), or an aromatic (W) residue. Our patch-clamp measurements show that with the exception of C76 and C311, the mutation of individual cytosolic cysteine to serine (S) did not significantly affect the single-channel conductance nor the channel open probability. However, mutating C76 to a charged or polar residue resulted either in an absence of channel activity or a decrease in open probability. In turn, the mutations C311S (polar), C311R (charged), and to a lesser degree C311A (aliphatic) led to an increase of the channel mean closed time due to the appearance of long closed time intervals (T(c) >or= 500 ms) and to a reduction of the reactivation by ATP of rundown Kir2.1 channels. These changes could be correlated with a weakening of the interaction between Kir2.1 and PIP(2), with C311R and C311S being more potent at modulating the Kir2.1-PIP(2) interaction than C311A. The present work supports, therefore, molecular models whereby the gating properties of Kir2.1 depend on the presence of nonpolar or neutral residues at positions 76 and 311, with C311 modulating the interaction between Kir2.1 and PIP(2).

Indexed as

AnimalsCell Membrane PermeabilityCells, CulturedCysteineCytosolHeLa CellsHumansIon Channel GatingMembrane PotentialsMutationOocytesPorosityPotassium Channels, Inwardly RectifyingProtein SubunitsRecombinant ProteinsStatic ElectricityCysteinePotassium Channels, Inwardly RectifyingProtein SubunitsRecombinant Proteins

Identifiers

PMID12770878
PMCPMC1302954
OpenAlexW1968714310

What OpenQuestion holds

Textmetadata
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.