Evidence map›Paper›PMID 22947928›Full record

ArticleBiophysical journal2012

Transfer of Kv3.1 voltage sensor features to the isolated Ci-VSP voltage-sensing domain.

Yukiko Mishina, Hiroki Mutoh, Thomas Knöpfel

Abstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Resource for FRET-Based Biosensor Optimization.Frontiers in cell and developmental biology · 2022
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Genetically Encoded Voltage Indicators: Opportunities and Challenges.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Divining the design principles of voltage sensors.The Journal of general physiology · 2014
    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.

Yukiko MishinaRIKEN Brain Science Institute, Saitama, Japan.
Hiroki Mutoh
Thomas Knöpfel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane proteins that respond to changes in transmembrane voltage are critical in regulating the function of living cells. The voltage-sensing domains (VSDs) of voltage-gated ion channels are extensively studied to elucidate voltage-sensing mechanisms, and yet many aspects of their structure-function relationship remain elusive. Here, we transplanted homologous amino acid motifs from the tetrameric voltage-activated potassium channel Kv3.1 to the monomeric VSD of Ciona intestinalis voltage-sensitive phosphatase (Ci-VSP) to explore which portions of Kv3.1 subunits depend on the tetrameric structure of Kv channels and which properties of Kv3.1 can be transferred to the monomeric Ci-VSP scaffold. By attaching fluorescent proteins to these chimeric VSDs, we obtained an optical readout to establish membrane trafficking and kinetics of voltage-dependent structural rearrangements. We found that motifs extending from 10 to roughly 100 amino acids can be readily transplanted from Kv3.1 into Ci-VSP to form engineered VSDs that efficiently incorporate into the plasma membrane and sense voltage. Some of the functional features of these engineered VSDs are reminiscent of Kv3.1 channels, indicating that these properties do not require interactions between Kv subunits or between the voltage sensing and the pore domains of Kv channels.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCiona intestinalisMolecular Sequence DataPC12 CellsPhosphoric Monoester HydrolasesPorosityProtein EngineeringProtein Structure, TertiaryRatsRecombinant Fusion ProteinsShaw Potassium ChannelsPhosphoric Monoester HydrolasesRecombinant Fusion ProteinsShaw Potassium Channelsvoltage-sensor-containing phosphatase, Ciona intestinalis

Identifiers

PMID22947928
PMCPMC3443783

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.