Evidence map›Paper›PMID 19959480›Full record

ArticleThe Journal of biological chemistry2010

Comparative study of the gating motif and C-type inactivation in prokaryotic voltage-gated sodium channels.

Katsumasa Irie, Kazuya Kitagawa, Hitoshi Nagura, Tomoya Imai, Takushi Shimomura, Yoshinori Fujiyoshi

Abstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

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  12. Sympathetic and parasympathetic innervation in cancer: therapeutic implications.Clinical autonomic research : official journal of the Clinical Autonomic Research Society · 2021
    Review
  13. Article
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  15. Article
  16. A Novel Single-Domain NaPlant physiology · 2020
    Article
  17. Article
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  20. Alternative Mechanisms for Fast NaCurrent biology : CB · 2019
    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

6 authors.

Katsumasa IrieFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502; the Japan Biological Informatics Consortium, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502, and.
Kazuya KitagawaFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502.
Hitoshi NaguraFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502.
Tomoya Imaithe Research Institute for Sustainable Humanosphere (RISH), Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
Takushi ShimomuraFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502.
Yoshinori FujiyoshiFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Oiwake, Kitashirakawa, Sakyo-ku, Kyoto 606-8502. Electronic address: yoshi@em.biophys.kyoto-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prokaryotic voltage-gated sodium channels (Na(V)s) are homotetramers and are thought to inactivate through a single mechanism, named C-type inactivation. Here we report the voltage dependence and inactivation rate of the NaChBac channel from Bacillus halodurans, the first identified prokaryotic Na(V), as well as of three new homologues cloned from Bacillus licheniformis (Na(V)BacL), Shewanella putrefaciens (Na(V)SheP), and Roseobacter denitrificans (Na(V)RosD). We found that, although activated by a lower membrane potential, Na(V)BacL inactivates as slowly as NaChBac. Na(V)SheP and Na(V)RosD inactivate faster than NaChBac. Mutational analysis of helix S6 showed that residues corresponding to the "glycine hinge" and "PXP motif" in voltage-gated potassium channels are not obligatory for channel gating in these prokaryotic Na(V)s, but mutations in the regions changed the inactivation rates. Mutation of the region corresponding to the glycine hinge in Na(V)BacL (A214G), Na(V)SheP (A216G), and NaChBac (G219A) accelerated inactivation in these channels, whereas mutation of glycine to alanine in the lower part of helix S6 in NaChBac (G229A), Na(V)BacL (G224A), and Na(V)RosD (G217A) reduced the inactivation rate. These results imply that activation gating in prokaryotic Na(V)s does not require gating motifs and that the residues of helix S6 affect C-type inactivation rates in these channels.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBacillusBacterial ProteinsCell LineCHO CellsCricetinaeCricetulusElectrophysiologyHumansIon Channel GatingMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedMutationBacterial ProteinsNaChBac protein, bacteriaSodium Channels

Identifiers

PMID19959480
PMCPMC2823509

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