Evidence map›Paper›PMID 17101817›Full record

ArticleThe Journal of general physiology2006

Constraints on voltage sensor movement in the shaker K+ channel.

Rachel B Darman, Allison A Ivy, Vina Ketty, Robert O Blaustein

Abstract read
In one paragraph

Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
–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

14 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Guideline
  2. Review
  3. The anthrax toxin channel: a barrel of LFs.The Journal of general physiology · 2011
    Article
  4. Article
  5. Article
  6. Potassium channel opening: a subtle two-step.The Journal of physiology · 2009
    Article
  7. The domain and conformational organization in potassium voltage-gated ion channels.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2009
    Review
  8. Review
  9. Review
  10. Tethering chemistry and K+ channels.The Journal of biological chemistry · 2008
    Review
  11. Article
  12. Article
  13. Article
  14. 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

4 authors.

Rachel B DarmanMolecular Cardiology Research Institute, Tufts-New England Medical Center, Boston, MA 02111, USA.
Allison A Ivy
Vina Ketty
Robert O Blaustein

Funding

Training Program in Cardiovascular ResearchT32HL069770 · NHLBI · TUFTS MEDICAL CENTER · PI KARAS, RICHARD H · 2003 to 2013
$4.7M
Structural Analysis of Voltage-gated Potassium ChannelsR01HL068985 · NHLBI · TUFTS MEDICAL CENTER · PI BLAUSTEIN, ROBERT O · 2003 to 2006
$1.3M
NHLBI NIH HHS R01 HL068985NHLBI NIH HHS R01HL68985NHLBI NIH HHS T32 HL069770NHLBI NIH HHS T32HL069770
6 · The paper itself

Abstract

In nerve and muscle cells, the voltage-gated opening and closing of cation-selective ion channels is accompanied by the translocation of 12-14 elementary charges across the membrane's electric field. Although most of these charges are carried by residues in the S4 helix of the gating module of these channels, the precise nature of their physical movement is currently the topic of spirited debate. Broadly speaking, two classes of models have emerged: those that suggest that small-scale motions can account for the extensive charge displacement, and those that invoke a much larger physical movement. In the most recent incarnation of the latter type of model, which is based on structural and functional data from the archaebacterial K(+) channel KvAP, a "voltage-sensor paddle" comprising a helix-turn-helix of S3-S4 translocates approximately 20 A through the bilayer during the gating cycle (Jiang, Y., A. Lee, J. Chen, V. Ruta, M. Cadene, B.T. Chait, and R. MacKinnon. 2003. Nature. 423:33-41; Jiang, Y., V. Ruta, J. Chen, A. Lee, and R. MacKinnon. 2003. Nature. 423:42-48.; Ruta, V., J. Chen, and R. MacKinnon. 2005. Cell. 123:463-475). We used two methods to test for analogous motions in the Shaker K(+) channel, each examining the aqueous exposure of residues near S3. In the first, we employed a pore-blocking maleimide reagent (Blaustein, R.O., P.A. Cole, C. Williams, and C. Miller. 2000. Nat. Struct. Biol. 7:309-311) to probe for state-dependent changes in the chemical reactivity of substituted cysteines; in the second, we tested the state-dependent accessibility of a tethered biotin to external streptavidin (Qiu, X.Q., K.S. Jakes, A. Finkelstein, and S.L. Slatin. 1994. J. Biol. Chem. 269:7483-7488; Slatin, S.L., X.Q. Qiu, K.S. Jakes, and A. Finkelstein. 1994. Nature. 371:158-161). In both types of experiments, residues predicted to lie near the top of S3 did not exhibit any change in aqueous exposure during the gating cycle. This lack of state dependence argues against large-scale movements, either axially or radially, of Shaker's S3-S4 voltage-sensor paddle.

Indexed as

Amino Acid SequenceAnimalsBiotinylationCysteineIon Channel GatingMolecular Sequence DataMovementOocytesShaker Superfamily of Potassium ChannelsStreptavidinXenopusCysteineShaker Superfamily of Potassium ChannelsStreptavidin

Identifiers

PMID17101817
PMCPMC2151604

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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.