Evidence map›Paper›PMID 10736307›Full record

ArticleThe Journal of general physiology2000

Permeation properties of inward-rectifier potassium channels and their molecular determinants.

H Choe, H Sackin, L G Palmer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

37 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. NBCe1-A is required for the renal ammonia and KAmerican journal of physiology. Renal physiology · 2020
    Article
  4. An in vitro analysis of intestinal ammonia transport in fasted and fed freshwater rainbow trout: roles of NKCC, KJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2019
    Article
  5. International journal of molecular sciences · 2019
    Review
  6. Article
  7. Epithelial transport inThe Journal of general physiology · 2017
    Review
  8. Review
  9. Aquaporin 4 as a NH3 Channel.The Journal of biological chemistry · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Potassium deprivation: a systems approach.American journal of physiology. Renal physiology · 2011
    Article
  14. A mathematical model of rat ascending Henle limb. II. Epithelial function.American journal of physiology. Renal physiology · 2010
    Article
  15. A mathematical model of rat ascending Henle limb. I. Cotransporter function.American journal of physiology. Renal physiology · 2010
    Article
  16. Cardiac strong inward rectifier potassium channels.Journal of molecular and cellular cardiology · 2010
    Review
  17. Article
  18. Review
  19. Article
  20. Molecular mechanisms of renal ammonia transport.Annual review of physiology · 2007
    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

3 authors at 2 institutions in 1 country.

H ChoeDepartment of Physiology, Weill Medical College of Cornell University, New York, New York 10021, USA.
H Sackin
L G Palmer
Cornell University · USRosalind Franklin University of Medicine and Science · US

Funding

MOLECULAR CLONING OF EPITHELIAL K CHANNELSR01DK046950 · NIDDK · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI SACKIN, HENRY · 1996 to 2017
$5.4M
MEMBRANE PROCESSES MEDIATING NACL TRANSPORTR01DK027847 · NIDDK · WEILL MEDICAL COLL OF CORNELL UNIV · PI PALMER, LAWRENCE G · 1986 to 2013
$4.8M
Molecular Cloning of Epithelial K ChannelsR56DK046950 · NIDDK · ROSALIND FRANKLIN UNIV OF MEDICINE & SCI · PI SACKIN, HENRY · 2008 to 2008
$231k
NIDDK NIH HHS DK27847NIDDK NIH HHS DK46950NIDDK NIH HHS R01 DK027847NIDDK NIH HHS R01 DK046950NIDDK NIH HHS R56 DK046950
6 · The paper itself

Abstract

The structural domains contributing to ion permeation and selectivity in K channels were examined in inward-rectifier K(+) channels ROMK2 (Kir1.1b), IRK1 (Kir2.1), and their chimeras using heterologous expression in Xenopus oocytes. Patch-clamp recordings of single channels were obtained in the cell-attached mode with different permeant cations in the pipette. For inward K(+) conduction, replacing the extracellular loop of ROMK2 with that of IRK1 increased single-channel conductance by 25 pS (from 39 to 63 pS), whereas replacing the COOH terminus of ROMK2 with that of IRK1 decreased conductance by 16 pS (from 39 to 22 pS). These effects were additive and independent of the origin of the NH(2) terminus or transmembrane domains, suggesting that the two domains form two resistors in series. The larger conductance of the extracellular loop of IRK1 was attributable to a single amino acid difference (Thr versus Val) at the 3P position, three residues in front of the GYG motif. Permeability sequences for the conducted ions were similar for the two channels: Tl(+) > K(+) > Rb(+) > NH(4)(+). The ion selectivity sequence for ROMK2 based on conductance ratios was NH(4)(+) (1.6) > K(+) (1) > Tl(+) (0.5) > Rb(+) (0.4). For IRK1, the sequence was K(+) (1) > Tl(+) (0.8) > NH(4)(+) (0.6) >> Rb(+) (0.1). The difference in the NH(4)(+)/ K(+) conductance (1.6) and permeability (0.09) ratios can be explained if NH(4)(+) binds with lower affinity than K(+) to sites within the pore. The relatively low conductances of NH(4)(+) and Rb(+) through IRK1 were again attributable to the 3P position within the P region. Site-directed mutagenesis showed that the IRK1 selectivity pattern required either Thr or Ser at this position. In contrast, the COOH-terminal domain conferred the relatively high Tl(+) conductance in IRK1. We propose that the P-region and the COOH terminus contribute independently to the conductance and selectivity properties of the pore.

Indexed as

Potassium Channels, Inwardly RectifyingAlgorithmsAmino Acid SequenceAnimalsCationsElectrophysiologyExtracellular SpaceIon Channel GatingModels, BiologicalMolecular Sequence DataOocytesPatch-Clamp TechniquesPermeabilityPlasmidsPotassium ChannelsRecombinant Fusion ProteinsCationsPotassium ChannelsPotassium Channels, Inwardly RectifyingRecombinant Fusion Proteins

Identifiers

PMID10736307
PMCPMC2233762
OpenAlexW2143785204

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.