Evidence map›Paper›PMID 15837928›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

The human Kv1.1 channel is palmitoylated, modulating voltage sensing: Identification of a palmitoylation consensus sequence.

Rose A Gubitosi-Klug, David J Mancuso, Richard W Gross

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022
    Review
  3. Review
  4. Palmitoylation Controls NMDA Receptor Function and Steroid Sensitivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  5. Article
  6. Article
  7. Palmitoylation of the KProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Full-Length P2XCell · 2019
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Ion channel regulation by protein S-acylation.The Journal of general physiology · 2014
    Review
  17. Article
  18. Article
  19. Article
  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 1 institution in 1 country.

Rose A Gubitosi-KlugDivision of Bioorganic Chemistry and Molecular Pharmacology, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA. rgross@wustl.edu
David J Mancuso
Richard W Gross
Washington University in St. Louis · US

Funding

LIPID MEDIATORS OF SIGNAL TRANSDUCTION IN SMOOTH MUSCLER01HL041250 · NHLBI · WASHINGTON UNIVERSITY · PI GROSS, RICHARD W · 1988 to 2011
$3.6M
NHLBI NIH HHS 5R01 HL 41250-12NHLBI NIH HHS R01 HL041250
6 · The paper itself

Abstract

Voltage-dependent K(+) channels rely on precise dynamic protein interactions with surrounding plasma membrane lipids to facilitate complex processes such as voltage sensing and channel gating. Many transmembrane-spanning proteins use palmitoylation to facilitate dynamic membrane interactions. Herein, we demonstrate that the human Kv1.1 ion channel is palmitoylated in the cytosolic portion of the S(2)-S(3) linker domain at residue C243. Through heterologous expression of the human Kv1.1 protein in Sf9 cells, covalent radiolabeling with [(3)H]palmitate, chemical stability studies of the [(3)H]-palmitoylated protein, and site-directed mutagenesis, C243 was identified as the predominant site of palmitoylation. The functional sequelae of palmitoylation were examined by analysis of whole cell currents from WT and mutant channels, which identified a 20-mV leftward shift in the current-voltage relationship when palmitoylation at C243 (but not with other cysteine deletions) is prevented by site-directed mutagenesis, implicating a role for palmitoylated C243 in modulating voltage sensing through protein-membrane interactions. Database searches identified an amino acid palmitoylation consensus motif (ACP/RSKT) that is present in multiple other members of the Shaker subfamily of K(+) channels and in several other unrelated regulatory proteins (e.g., CD36, nitric oxide synthase type 2, and the mannose-6 phosphate receptor) that are known to be palmitoylated by thioester linkages at the predicted consensus site cysteine residue. Collectively, these results (i) identify palmitoylation as a mechanism for K(+) channel interactions with plasma membrane lipids contributing to electric field-induced conformational alterations, and ii) define an amino acid consensus sequence for protein palmitoylation.

Indexed as

AnimalsCell LineCloning, MolecularConsensus SequenceHumansKineticsKv1.1 Potassium ChannelMembrane LipidsMembrane PotentialsMutagenesis, Site-DirectedPalmitic AcidPatch-Clamp TechniquesPotassium Channels, Voltage-GatedProtein ConformationRecombinant ProteinsSpodopteraKCNA1 protein, humanKv1.1 Potassium ChannelMembrane LipidsPalmitic AcidPotassium Channels, Voltage-GatedRecombinant Proteins

Identifiers

PMID15837928
PMCPMC1087951
OpenAlexW2076996214

What OpenQuestion holds

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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.