Evidence map›Paper›PMID 17766348›Full record

ArticleBiophysical journal2007

An activation gating switch in Kv1.2 is localized to a threonine residue in the S2-S3 linker.

Saman Rezazadeh, Harley T Kurata, Thomas W Claydon, Steven J Kehl, David Fedida

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Competitive modulation of KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
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  8. Of Seven New KToxins · 2023
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  9. An activator of voltage-gated KProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Article
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  13. A NovelInternational journal of molecular sciences · 2021
    Article
  14. Article
  15. Slc7a5 alters Kvβ-mediated regulation of Kv1.2.The Journal of general physiology · 2020
    Article
  16. Article
  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

5 authors at 1 institution in 1 country.

Saman RezazadehDepartment of Anesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.
Harley T Kurata
Thomas W Claydon
Steven J Kehl
David Fedida
University of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activation properties of Kv1.2 channels are highly variable, with reported half-activation (V((1/2))) values ranging from approximately -40 mV to approximately +30 mV. Here we show that this arises because Kv1.2 channels occupy two distinct gating modes ("fast" and "slow"). "Slow" gating (tau(act) = 90 +/- 6 ms at +35 mV) was associated with a V((1/2)) of activation of +16.6 +/- 1.1 mV, whereas "fast" gating (tau(act) = 4.5 +/- 1.7 ms at +35 mV) was associated with a V((1/2)) of activation of -18.8 +/- 2.3 mV. It was possible to switch between gating modes by applying a prepulse, which suggested that channels activate to a single open state along separate "fast" and "slow" activation pathways. Using chimeras and point mutants between Kv1.2 and Kv1.5 channels, we determined that introduction of a positive charge at or around threonine 252 in the S2-S3 linker of Kv1.2 abolished "slow" activation gating. Furthermore, dialysis of the cytoplasm or excision of cell-attached patches from cells expressing Kv1.2 channels switched gating from "slow" to "fast", suggesting involvement of cytoplasmic regulators. Collectively, these results demonstrate two modes of activation gating in Kv1.2 and specific residues in the S2-S3 linker that act as a switch between these modes.

Indexed as

Amino Acid SubstitutionCell LineHumansIon Channel GatingKidneyKv1.2 Potassium ChannelStructure-Activity RelationshipThreonineKv1.2 Potassium ChannelThreonine

Identifiers

PMID17766348
PMCPMC2098734
OpenAlexW2066433833

What OpenQuestion holds

Textmetadata
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.