Evidence map›Paper›PMID 25285449›Full record

ArticleeLife2014

Phosphatidic acid modulation of Kv channel voltage sensor function.

Richard K Hite, Joel A Butterwick, Roderick MacKinnon

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.1field-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

41 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Lipid probes to study ion channels.Current opinion in chemical biology · 2025
    Review
  4. Fluctuating hydrogen-bond network of the Hv1 ion channel.Computational and structural biotechnology journal · 2025
    Article
  5. Competitive modulation of KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Voltage-sensor movements in the Eag Kv channel under an applied electric field.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Slc7a5 alters Kvβ-mediated regulation of Kv1.2.The Journal of general physiology · 2020
    Article
  18. Article
  19. Review
  20. 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

3 authors at 2 institutions in 1 country.

Richard K HiteLaboratory of Molecular Neurobiology and Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, United States.
Joel A ButterwickLaboratory of Molecular Neurobiology and Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, United States.
Roderick MacKinnonLaboratory of Molecular Neurobiology and Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, United States.
Rockefeller University · USHoward Hughes Medical Institute · US

Funding

Voltage-Dependent Ion Channel GatingR01GM043949 · NIGMS · ROCKEFELLER UNIVERSITY · PI MACKINNON, RODERICK · 1990 to 2024
$10.1M
Howard Hughes Medical InstituteNIGMS NIH HHS GM43949NIGMS NIH HHS R01 GM043949
6 · The paper itself

Abstract

Membrane phospholipids can function as potent regulators of ion channel function. This study uncovers and investigates the effect of phosphatidic acid on Kv channel gating. Using the method of reconstitution into planar lipid bilayers, in which protein and lipid components are defined and controlled, we characterize two effects of phosphatidic acid. The first is a non-specific electrostatic influence on activation mediated by electric charge density on the extracellular and intracellular membrane surfaces. The second is specific to the presence of a primary phosphate group, acts only through the intracellular membrane leaflet and depends on the presence of a particular arginine residue in the voltage sensor. Intracellular phosphatidic acid accounts for a nearly 50 mV shift in the midpoint of the activation curve in a direction consistent with stabilization of the voltage sensor's closed conformation. These findings support a novel mechanism of voltage sensor regulation by the signaling lipid phosphatidic acid.

Indexed as

AdenosineAmino Acid SequenceAnimalsGlycerophospholipidsIon Channel GatingLipid BilayersMolecular Sequence DataPhosphatidic AcidsPhosphatidylcholinesPhospholipase DPotassium Channels, Voltage-GatedRatsSequence Alignment1,2-diphytanoylphosphatidylcholine1-palmitoyl-2-oleoyl-phosphatidyl-3-adenosineAdenosineGlycerophospholipidsLipid BilayersPhosphatidic AcidsPhosphatidylcholinesPhospholipase Dphospholipase D1Potassium Channels, Voltage-Gatedbiophysicselectrophysiologyion channelsratstructural biologyvoltage-gated potassium channels

Identifiers

PMID25285449
PMCPMC4212207
OpenAlexW2129537918

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.