Evidence map›Paper›PMID 22802363›Full record

ArticleThe Journal of general physiology2012

Engineered interaction between SUR1 and Kir6.2 that enhances ATP sensitivity in KATP channels.

Emily B Pratt, Qing Zhou, Joel W Gay, Show-Ling Shyng

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

24 citing papers in PubMed, 40 citations in OpenAlex.

  1. Inhibition Mechanism of Pancreatic KResearch (Washington, D.C.) · 2026
    Article
  2. Dynamic duo: Kir6 and SUR in KChannels (Austin, Tex.) · 2024
    Review
  3. HCV affects KEndocrine · 2024
    Article
  4. Structure of an open KNature communications · 2024
    Article
  5. Electro-metabolic signaling.The Journal of general physiology · 2024
    Article
  6. KCurrent opinion in structural biology · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Molecular structure of an open human KProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Development of IFrontiers in pharmacology · 2021
    Article
  12. Article
  13. New insights into KNature reviews. Endocrinology · 2020
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Emily B PrattDepartment of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97239, USA. pratte@ohsu.edu
Qing Zhou
Joel W Gay
Show-Ling Shyng
Oregon Health & Science University · US

Funding

Structural Basis of KATP Channel GatingR01DK066485 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SHYNG, SHOW-LING · 2006 to 2024
$5.8M
SUR1 mutations and Subunit Associations in ATP-Sensitive Potassium ChannelsF30DK081305 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI PRATT, EMILY B · 2008 to 2011
$178k
NIDDK NIH HHS DK066485-05NIDDK NIH HHS F30 DK081305NIDDK NIH HHS F30DK081305NIDDK NIH HHS R01 DK066485
6 · The paper itself

Abstract

The ATP-sensitive potassium (K(ATP)) channel consisting of the inward rectifier Kir6.2 and SUR1 (sulfonylurea receptor 1) couples cell metabolism to membrane excitability and regulates insulin secretion. Inhibition by intracellular ATP is a hallmark feature of the channel. ATP sensitivity is conferred by Kir6.2 but enhanced by SUR1. The mechanism by which SUR1 increases channel ATP sensitivity is not understood. In this study, we report molecular interactions between SUR1 and Kir6.2 that markedly alter channel ATP sensitivity. Channels bearing an E203K mutation in SUR1 and a Q52E in Kir6.2 exhibit ATP sensitivity ∼100-fold higher than wild-type channels. Cross-linking of E203C in SUR1 and Q52C in Kir6.2 locks the channel in a closed state and is reversible by reducing agents, demonstrating close proximity of the two residues. Our results reveal that ATP sensitivity in K(ATP) channels is a dynamic parameter dictated by interactions between SUR1 and Kir6.2.

Indexed as

Adenosine TriphosphateAmino Acid SubstitutionAnimalsATP-Binding Cassette TransportersChlorocebus aethiopsCOS CellsCricetinaeCricetulusIon Channel GatingKATP ChannelsKcnj11 ChannelPotassiumPotassium Channels, Inwardly RectifyingProtein Interaction Domains and MotifsRatsReceptors, DrugAbcc8 protein, ratAdenosine TriphosphateATP-Binding Cassette TransportersKATP ChannelsKcnj11 ChannelPotassiumPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea Receptors

Identifiers

PMID22802363
PMCPMC3409095
OpenAlexW2109895718

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.