Evidence map›Paper›PMID 12881418›Full record

ArticleThe EMBO journal2003

N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits.

Kim W Chan, Hailin Zhang, Diomedes E Logothetis

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

91 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. Article
  3. Dynamic duo: Kir6 and SUR in KChannels (Austin, Tex.) · 2024
    Review
  4. Article
  5. Structure of an open KNature communications · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. KFrontiers in endocrinology · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

31 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Kim W ChanDepartment of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, New York, NY 10029, USA. kwc8@po.cwru.edu
Hailin Zhang
Diomedes E Logothetis
New York University · US

Funding

Structural Determinants of PIP2 RegulationR01HL059949 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Leigh Daniel Plant · 1998 to 2026
$11.6M
SUR Transmembrane Domain in K(ATP) Channel FunctionR01DK060104 · NIDDK · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI HARVEY, ROBERT D · 2002 to 2006
$1.2M
NHLBI NIH HHS HL59949NHLBI NIH HHS R01 HL059949NIDDK NIH HHS DK60104NIDDK NIH HHS R01 DK060104
6 · The paper itself

Abstract

The sulfonylurea receptor (SUR), an ATP-binding cassette (ABC) protein, assembles with a potassium channel subunit (Kir6) to form the ATP-sensitive potassium channel (K(ATP)) complex. Although SUR is an important regulator of Kir6, the specific SUR domain that associates with Kir6 is still unknown. All functional ABC proteins contain two transmembrane domains but some, including SUR and MRP1 (multidrug resistance protein 1), contain an extra N-terminal transmembrane domain called TMD0. The functions of any TMD0s are largely unclear. Using Xenopus oocytes to coexpress truncated SUR constructs with Kir6, we demonstrated by immunoprecipitation, single-oocyte chemiluminescence and electrophysiological measurements that the TMD0 of SUR1 strongly associated with Kir6.2 and modulated its trafficking and gating. Two TMD0 mutations, A116P and V187D, previously correlated with persistent hyperinsulinemic hypoglycemia of infancy, were found to disrupt the association between TMD0 and Kir6.2. These results underscore the importance of TMD0 in K(ATP) channel function, explaining how specific mutations within this domain result in disease, and suggest how an ABC protein has evolved to regulate a potassium channel.

Indexed as

ATP-Binding Cassette TransportersIon Channel GatingAdenosine DiphosphateAdenosine TriphosphateAnimalsDiazoxideGlyburideMutagenesis, Site-DirectedPotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea ReceptorsXenopusAdenosine DiphosphateAdenosine TriphosphateATP-Binding Cassette TransportersDiazoxideGlyburidePotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, DrugSulfonylurea Receptors

Identifiers

PMID12881418
PMCPMC169049
OpenAlexW2016061230

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.