Evidence map›Paper›PMID 23197389›Full record

ArticleProteomics2013

Comparative proteomic analysis of the ATP-sensitive K+ channel complex in different tissue types.

Eirini Kefaloyianni, John S Lyssand, Cesar Moreno, Diane Delaroche, Miyoun Hong, David Fenyö, Charles V Mobbs, Thomas A Neubert, William A Coetzee

Abstract read
In one paragraph

Article in Proteomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. KArhiv za farmaciju · 2024
    Article
  3. KScientific reports · 2022
    Article
  4. Article
  5. Ion Transporters, Channelopathies, and Glucose Disorders.International journal of molecular sciences · 2019
    Review
  6. The trafficking protein, EHD2, positively regulates cardiac sarcolemmal KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Cardiovascular KPathobiology of aging & age related diseases · 2016
    Review
  13. KATP Channels in the Cardiovascular System.Physiological reviews · 2016
    Review
  14. Review
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

9 authors.

Eirini KefaloyianniPediatrics, NYU School of Medicine, New York, NY 10016, USA.
John S Lyssand
Cesar Moreno
Diane Delaroche
Miyoun Hong
David Fenyö
Charles V Mobbs
Thomas A Neubert
William A Coetzee

Funding

Training Program in NeuroscienceT32MH087004 · NIMH · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI GEORGE W. HUNTLEY · 2009 to 2026
$4.0M
Potassium Channels as Macromolecular ComplexesR01HL085820 · NHLBI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COETZEE, WILLIAM A, NEUBERT, THOMAS A · 2008 to 2013
$3.2M
NHLBI NIH HHS HL085820NHLBI NIH HHS R01 HL085820NIMH NIH HHS T32 MH087004
6 · The paper itself

Abstract

ATP-sensitive K(+) (K(ATP)) channels are expressed ubiquitously, but have diverse roles in various organs and cells. Their diversity can partly be explained by distinct tissue-specific compositions of four copies of the pore-forming inward rectifier potassium channel subunits (Kir6.1 and/or Kir6.2) and four regulatory sulfonylurea receptor subunits (SUR1 and/or SUR2). Channel function and/or subcellular localization also can be modified by the proteins with which they transiently or permanently interact to generate even more diversity. We performed a quantitative proteomic analysis of K(ATP) channel complexes in the heart, endothelium, insulin-secreting min6 cells (pancreatic β-cell like), and the hypothalamus to identify proteins with which they interact in different tissues. Glycolysis is an overrepresented pathway in identified proteins of the heart, min6 cells, and the endothelium. Proteins with other energy metabolic functions were identified in the hypothalamic samples. These data suggest that the metabolo-electrical coupling conferred by K(ATP) channels is conferred partly by proteins with which they interact. A large number of identified cytoskeletal and trafficking proteins suggests endocytic recycling may help control K(ATP) channel surface density and/or subcellular localization. Overall, our data demonstrate that K(ATP) channels in different tissues may assemble with proteins having common functions, but that tissue-specific complex organization also occurs.

Indexed as

AnimalsATP-Binding Cassette TransportersEndotheliumInsulin-Secreting CellsKATP ChannelsMiceMyocardiumOrgan SpecificityPotassium Channels, Inwardly RectifyingProteomicsReceptors, DrugSulfonylurea ReceptorsAbcc8 protein, mouseATP-Binding Cassette TransportersKATP ChannelsPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea Receptors

Identifiers

PMID23197389
PMCPMC3717560

What OpenQuestion holds

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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.