Evidence map›Paper›PMID 26931497›Full record

ArticleScientific reports2016

Caveolin interaction governs Kv1.3 lipid raft targeting.

Mireia Pérez-Verdaguer, Jesusa Capera, Ramón Martínez-Mármol, Marta Camps, Núria Comes, Michael M Tamkun, Antonio Felipe

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

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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

26 citing papers in PubMed.

  1. Review
  2. Article
  3. Identification of Novel Kv1.3 Channel-Interacting Proteins Using Proximity Labelling in T-Cells.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2025
    Article
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  5. Review
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  7. Article
  8. Review
  9. A Meta-Analysis Study to Infer Voltage-Gated KAntioxidants (Basel, Switzerland) · 2023
    Article
  10. Article
  11. Article
  12. Chemical editing of proteoglycan architecture.Nature chemical biology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

7 authors.

Mireia Pérez-VerdaguerMolecular Physiology Laboratory, Universitat de Barcelona, 08028 Barcelona, Spain.
Jesusa CaperaMolecular Physiology Laboratory, Universitat de Barcelona, 08028 Barcelona, Spain.
Ramón Martínez-MármolMolecular Physiology Laboratory, Universitat de Barcelona, 08028 Barcelona, Spain.
Marta CampsInstitut de Biomedicina (IBUB). Departament de Bioquímica i Biologia Molecular. Universitat de Barcelona, 08028 Barcelona, Spain.
Núria ComesMolecular Physiology Laboratory, Universitat de Barcelona, 08028 Barcelona, Spain.
Michael M TamkunDepartment of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
Antonio FelipeMolecular Physiology Laboratory, Universitat de Barcelona, 08028 Barcelona, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spatial localization of ion channels at the cell surface is crucial for their functional role. Many channels localize in lipid raft microdomains, which are enriched in cholesterol and sphingolipids. Caveolae, specific lipid rafts which concentrate caveolins, harbor signaling molecules and their targets becoming signaling platforms crucial in cell physiology. However, the molecular mechanisms involved in such spatial localization are under debate. Kv1.3 localizes in lipid rafts and participates in the immunological response. We sought to elucidate the mechanisms of Kv1.3 surface targeting, which govern leukocyte physiology. Kv1 channels share a putative caveolin-binding domain located at the intracellular N-terminal of the channel. This motif, lying close to the S1 transmembrane segment, is situated near the T1 tetramerization domain and the determinants involved in the Kvβ subunit association. The highly hydrophobic domain (FQRQVWLLF) interacts with caveolin 1 targeting Kv1.3 to caveolar rafts. However, subtle variations of this cluster, putative ancillary associations and different structural conformations can impair the caveolin recognition, thereby altering channel's spatial localization. Our results identify a caveolin-binding domain in Kv1 channels and highlight the mechanisms that govern the regulation of channel surface localization during cellular processes.

Indexed as

Amino Acid SequenceBiopolymersCaveolinsHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsKv1.3 Potassium ChannelMembrane MicrodomainsProtein BindingBiopolymersCaveolinsKv1.3 Potassium Channel

Identifiers

PMID26931497
PMCPMC4773814

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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.