Evidence map›Paper›PMID 18794864›Full record

ArticleNature chemical biology2008

A sodium-mediated structural switch that controls the sensitivity of Kir channels to PtdIns(4,5)P(2).

Avia Rosenhouse-Dantsker, Jin L Sui, Qi Zhao, Radda Rusinova, Aldo A Rodríguez-Menchaca, Zhe Zhang, Diomedes E Logothetis

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

29 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. The Role of KCells · 2024
    Review
  3. From Crosstalk to Synergism: The Combined Effect of Cholesterol and PI(4,5)PAdvances in experimental medicine and biology · 2023
    Review
  4. Oxidation Driven Reversal of PIPFunction (Oxford, England) · 2023
    Article
  5. PI(4,5)PAdvances in experimental medicine and biology · 2023
    Article
  6. Article
  7. Review
  8. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  9. Expression, localization, and functional properties of inwardly rectifying KAmerican journal of physiology. Renal physiology · 2020
    Review
  10. Article
  11. Article
  12. A Critical Gating Switch at a Modulatory Site in Neuronal Kir3 Channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  13. Article
  14. Article
  15. Review
  16. 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

7 authors at 4 institutions in 1 country.

Avia Rosenhouse-DantskerDepartment of Structural and Chemical Biology, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, New York 10029, USA.
Jin L Sui
Qi Zhao
Radda Rusinova
Aldo A Rodríguez-Menchaca
Zhe Zhang
Diomedes E Logothetis
Cornell University · USVirginia Commonwealth University Medical Center · USIcahn School of Medicine at Mount Sinai · USMount Sinai Hospital · US

Funding

Structural Determinants of PIP2 RegulationR01HL059949 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Leigh Daniel Plant · 1998 to 2026
$11.6M
NHLBI NIH HHS HL-59949NHLBI NIH HHS R01 HL059949
6 · The paper itself

Abstract

Inwardly rectifying potassium (Kir) channels are gated by the membrane phospholipid phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P(2)). Among them, Kir3 requires additional molecules, such as the betagamma subunits of G proteins or intracellular sodium, for channel gating. Using an interactive computational-experimental approach, we show that sodium sensitivity of Kir channels involves the side chains of an aspartate and a histidine located across from each other in a crucial loop in the cytosolic domain, as well as the backbone carbonyls of two more residues and a water molecule. The location of the coordination site in the vicinity of a conserved arginine shown to affect channel-PtdIns(4,5)P(2) interactions suggests that sodium triggers a structural switch that frees the crucial arginine. Mutations of the aspartate and the histidine that affect sodium sensitivity also enhance the channel's sensitivity to PtdIns(4,5)P(2). Furthermore, on the basis of the molecular characteristics of the coordination site, we identify and confirm experimentally a sodium-sensitive phenotype in Kir5.1.

Indexed as

Amino Acid SequenceComputer SimulationG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIon Channel GatingIonsModels, MolecularMolecular Sequence DataPhosphatidylinositol 4,5-DiphosphateSequence AlignmentSodiumG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIonsPhosphatidylinositol 4,5-DiphosphateSodium

Identifiers

PMID18794864
PMCPMC4100997
OpenAlexW2085882081

What OpenQuestion holds

Textmetadata
LicenceTDM
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.