Evidence map›Paper›PMID 12407074›Full record

ArticleThe Journal of general physiology2002

Hydrolyzable ATP and PIP(2) modulate the small-conductance K+ channel in apical membranes of rat cortical-collecting duct (CCD).

Ming Lu, Steven C Hebert, Gerhard Giebisch

Abstract read
In one paragraph

Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Review
  3. Striking a balance: PIPExploration of neuroprotective therapy · 2021
    Article
  4. Article
  5. PIPProceedings of the National Academy of Sciences of the United States of America · 2020
    Review
  6. Review
  7. Article
  8. Phosphoinositides regulate ion channels.Biochimica et biophysica acta · 2015
    Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Regulation of potassium (K) handling in the renal collecting duct.Pflugers Archiv : European journal of physiology · 2009
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Gating mechanism of KATP channels: function fits form.The Journal of general physiology · 2003
    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.

Ming LuDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520, USA. ming.lu@yale.edu
Steven C Hebert
Gerhard Giebisch

Funding

STRUCTURE AND FUNCTION OF ROMK CHANNEL IN KIDNEYR01DK054999 · NIDDK · YALE UNIVERSITY · PI WANG, TONG WANG · 2001 to 2008
$3.2M
ROMK CHANNEL FUNCTION AND REGULATION IN KIDNEYR01DK054998 · NIDDK · YALE UNIVERSITY · PI GIEBISCH, GERHARD H · 1999 to 2003
$883k
NIDDK NIH HHS R01 DK054998NIDDK NIH HHS R01 DK054999
6 · The paper itself

Abstract

The small-conductance K+ channel (SK) in the apical membrane of the cortical-collecting duct (CCD) is regulated by adenosine triphosphate (ATP) and phosphorylation-dephosphorylation processes. When expressed in Xenopus oocytes, ROMK, a cloned K+ channel similar to the native SK channel, can be stimulated by phosphatidylinositol bisphosphate (PIP2), which is produced by phosphoinositide kinases from phosphatidylinositol. However, the effects of PIP2 on SK channel activity are not known. In the present study, we investigated the mechanism by which hydrolyzable ATP prevented run-down of SK channel activity in excised apical patches of principal cells from rat CCD. Channel run-down was significantly delayed by pretreatment with hydrolyzable Mg-ATP, but ATP gamma S and AMP-PNP had no effect. Addition of alkaline phosphatase also resulted in loss of channel activity. After run-down, SK channel activity rapidly increased upon addition of PIP2. Exposure of inside-out patches to phosphoinositide kinase inhibitors (LY294002, quercetin or wortmannin) decreased channel activity by 74% in the presence of Mg-ATP. PIP2 added to excised patches reactivated SK channels in the presence of these phosphoinositide kinase inhibitors. The protein kinase A inhibitor, PKI, reduced channel activity by 36% in the presence of Mg-ATP. PIP2 was also shown to modulate the inhibitory effects of extracellular and cytosolic ATP. We conclude that both ATP-dependent formation of PIP2 through membrane-bound phosphoinositide kinases and phosphorylation of SK by PKA play important roles in modulating SK channel activity.

Indexed as

1-Phosphatidylinositol 4-KinaseAdenosine TriphosphateAnimalsCell MembraneCyclic AMP-Dependent Protein KinasesElectrophysiologyHydrolysisKidney CortexKidney Tubules, CollectingKineticsMembrane PotentialsPatch-Clamp TechniquesPhosphatidylinositol 4,5-DiphosphatePhosphorylationPotassium ChannelsPotassium Channels, Inwardly Rectifying1-Phosphatidylinositol 4-KinaseAdenosine TriphosphateCyclic AMP-Dependent Protein KinasesKcnj1 protein, ratPhosphatidylinositol 4,5-DiphosphatePotassium ChannelsPotassium Channels, Inwardly Rectifying

Identifiers

PMID12407074
PMCPMC2229550

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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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.