Evidence map›Paper›PMID 21244834›Full record

ArticleBiophysical journal2011

Cholesterol sensitivity of KIR2.1 is controlled by a belt of residues around the cytosolic pore.

Avia Rosenhouse-Dantsker, Diomedes E Logothetis, Irena Levitan

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. PI(4,5)PAdvances in experimental medicine and biology · 2023
    Article
  7. Cholesterol and PIPAdvances in experimental medicine and biology · 2023
    Article
  8. From Crosstalk to Synergism: The Combined Effect of Cholesterol and PI(4,5)PAdvances in experimental medicine and biology · 2023
    Review
  9. Article
  10. A molecular switch controls the impact of cholesterol on a Kir channel.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Defining how multiple lipid species interact with inward rectifier potassium (Kir2) channels.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. 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 at 2 institutions in 1 country.

Avia Rosenhouse-DantskerDepartment of Medicine, University of Illinois at Chicago, USA. dantsker@uic.edu
Diomedes E Logothetis
Irena Levitan
University of Illinois Chicago · USVirginia Commonwealth University · US

Funding

Structural Determinants of PIP2 RegulationR01HL059949 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Leigh Daniel Plant · 1998 to 2026
$11.6M
Cholesterol Regulation of Endothelial K+ ChannelsR01HL073965 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI LEVITAN, IRENA · 2004 to 2024
$7.3M
Impact of dyslipidemia on endothelial biomechanicsR01HL083298 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LEVITAN, IRENA, MINSHALL, RICHARD D · 2007 to 2021
$7.0M
Modulation of Kir Channel Function by PhosphorylationR01HL090882 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI LOGOTHETIS, DIOMEDES E. · 2009 to 2012
$1.5M
NHLBI NIH HHS HL-059949NHLBI NIH HHS HL-073965NHLBI NIH HHS HL-083298NHLBI NIH HHS HL-090882NHLBI NIH HHS R01 HL059949NHLBI NIH HHS R01 HL073965NHLBI NIH HHS R01 HL083298NHLBI NIH HHS R01 HL090882
6 · The paper itself

Abstract

Kir channels play an important role in setting the resting membrane potential and modulating membrane excitability. A common feature of several Kir channels is that they are regulated by cholesterol. Yet, the mechanism by which cholesterol affects channel function is unclear. We recently showed that the cholesterol sensitivity of Kir2 channels depends on several CD-loop residues. Here we show that this cytosolic loop is part of a regulatory site that also includes residues in the G-loop, the N-terminus, and the connecting segment between the C-terminus and the inner transmembrane helix. Together, these residues form a cytosolic belt that surrounds the pore of the channel close to its interface with the transmembrane domain, and modulate the cholesterol sensitivity of the channel. Furthermore, we show that residues in this cluster are correlated with residues located in the most flexible region of the G-loop, the major cytosolic gate of Kir2.1, implying that the importance of these residues extends beyond their effect on the channel's cholesterol sensitivity. We suggest that the residues of the cholesterol sensitivity belt are critical for channel gating.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsBinding SitesCholesterolCytosolIon Channel GatingMembrane PotentialsMolecular Sequence DataOocytesPotassium Channels, Inwardly RectifyingProtein Structure, TertiaryXenopusCholesterolKir2.1 channelPotassium Channels, Inwardly Rectifying

Identifiers

PMID21244834
PMCPMC3021658
OpenAlexW2020185913

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.