Evidence map›Paper›PMID 19783984›Full record

ArticleNature structural & molecular biology2009

Interactions between lipids and voltage sensor paddles detected with tarantula toxins.

Mirela Milescu, Frank Bosmans, Seungkyu Lee, AbdulRasheed A Alabi, Jae Il Kim, Kenton J Swartz

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

94 citing papers in PubMed, 140 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Mechanism of use-dependent Kv2 channel inhibition by RY785.The Journal of general physiology · 2022
    Article
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  8. Multitarget nociceptor sensitization by a promiscuous peptide from the venom of the King Baboon spider.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. Article
  11. Review
  12. Pain-related toxins in scorpion and spider venoms: a face to face with ion channels.The journal of venomous animals and toxins including tropical diseases · 2021
    Review
  13. Peptide Toxins Targeting KV Channels.Handbook of experimental pharmacology · 2021
    Review
  14. Tracking the motion of the KThe Journal of physiology · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

34 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 3 countries.

Mirela MilescuMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland, USA. Mirela.Milescu@nih.gov
Frank Bosmans
Seungkyu Lee
AbdulRasheed A Alabi
Jae Il Kim
Kenton J Swartz
National Institute of Neurological Disorders and Stroke · USGwangju Institute of Science and Technology · KRKU Leuven · BE

Funding

Gating mechanisms and pharmacology of voltage-activated ion channelsZIANS002945 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2009 to 2025
$44.2M
Intramural NIH HHS ZIA NS002945
6 · The paper itself

Abstract

Voltage-activated ion channels open and close in response to changes in voltage, a property that is essential for generating nerve impulses. Studies on voltage-activated potassium (Kv) channels show that voltage-sensor activation is sensitive to the composition of lipids in the surrounding membrane. Here we explore the interaction of lipids with S1-S4 voltage-sensing domains and find that the conversion of the membrane lipid sphingomyelin to ceramide-1-phosphate alters voltage-sensor activation in an S1-S4 voltage-sensing protein lacking an associated pore domain, and that the S3b-S4 paddle motif determines the effects of lipid modification on Kv channels. Using tarantula toxins that bind to paddle motifs within the membrane, we identify mutations in the paddle motif that weaken toxin binding by disrupting lipid-paddle interactions. Our results suggest that lipids bind to voltage-sensing domains and demonstrate that the pharmacological sensitivities of voltage-activated ion channels are influenced by the surrounding lipid membrane.

Indexed as

AnimalsCell MembraneCrystallography, X-RayIon Channel GatingIon ChannelsLipidsModels, BiologicalPhosphoric Diester HydrolasesPhosphoric Monoester HydrolasesShab Potassium ChannelsSphingomyelinsSpidersSpider VenomsSurface PropertiesThermodynamicsIon ChannelsLipidsPhosphoric Diester HydrolasesPhosphoric Monoester HydrolasesShab Potassium Channelssphingomyelin phosphodiesterase DSphingomyelinsSpider Venoms

Identifiers

PMID19783984
PMCPMC2782670
OpenAlexW2047433025

What OpenQuestion holds

Textmetadata
LicenceTDM
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.