Evidence map›Paper›PMID 18463315›Full record

ArticleAmerican journal of physiology. Renal physiology2008

MiRP3 acts as an accessory subunit with the BK potassium channel.

Daniel I Levy, Sherry Wanderling, Daniel Biemesderfer, Steve A N Goldstein

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Renal physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Novel exon 1 protein-coding regions N-terminally extend human KCNE3 and KCNE4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  8. Kcne4 deletion sex- and age-specifically impairs cardiac repolarization in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  9. Article
  10. Review
  11. Role of BK channels in hypertension and potassium secretion.Current opinion in nephrology and hypertension · 2011
    Review
  12. A novel auxiliary subunit critical to BK channel function in Caenorhabditis elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Daniel I LevyDepartment of Medicine, Biological Sciences Division, University of Chicago, Chicago, Illinois, USA. dlevy@medicine.bsd.uchicago.edu
Sherry Wanderling
Daniel Biemesderfer
Steve A N Goldstein
University of Chicago · US

Funding

MinK-related peptides(MiRPs): structure and functionR01GM051851 · NIGMS · YALE UNIVERSITY · PI GOLDSTEIN, STEVE A N · 1996 to 2004
$2.2M
NIGMS NIH HHS R01 GM051851
6 · The paper itself

Abstract

MinK-related peptides (MiRPs) are single-span membrane proteins that assemble with specific voltage-gated K+ (Kv) channel alpha-subunits to establish gating kinetics, unitary conductance, expression level, and pharmacology of the mixed complex. MiRP3 (encoded by the KCNE4 gene) has been shown to alter the behavior of some Kv alpha-subunits in vitro but its natural partners and physiologic functions are unknown. Seeking in vivo partners for MiRP3, immunohistochemistry was used to localize its expression to a unique subcellular site, the apical membrane of renal intercalated cells, where one potassium channel type has been recorded, the calcium- and voltage-gated channel BK. Overlapping staining of these two proteins was found in rabbit intercalated cells, and MiRP3 and BK subunits expressed in tissue culture cells were found to form detergent-stable complexes. Electrophysiologic and biochemical evaluation showed MiRP3 to act on BK to reduce current density in two fashions: shifting the current-voltage relationship to more depolarized voltages in a calcium-dependent fashion ( approximately 10 mV at normal intracellular calcium levels) and accelerating degradation of MiRP3-BK complexes. The findings suggest a role for MiRP3 modulation of BK-dependent urinary potassium excretion.

Indexed as

AnimalsChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusHumansKidneyLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsOocytesPatch-Clamp TechniquesPotassiumPotassium Channels, Voltage-GatedProtein SubunitsRabbitsKCNE4 protein, humanKCNE4 protein, ratLarge-Conductance Calcium-Activated Potassium ChannelsPotassiumPotassium Channels, Voltage-GatedProtein Subunits

Identifiers

PMID18463315
PMCPMC2519185
OpenAlexW2049239874

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.