Evidence map›Paper›PMID 30484774›Full record

ArticleeLife2018

The hydrophobic nature of a novel membrane interface regulates the enzyme activity of a voltage-sensing phosphatase.

Akira Kawanabe, Masaki Hashimoto, Manami Nishizawa, Kazuhisa Nishizawa, Hirotaka Narita, Tomoko Yonezawa, Yuka Jinno, Souhei Sakata, Atsushi Nakagawa, Yasushi Okamura

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Nonsubstrate PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Interaction between S4 and the phosphatase domain mediates electrochemical coupling in voltage-sensing phosphatase (VSP).Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Engineering an enhanced voltage-sensing phosphatase.The Journal of general physiology · 2020
    Article
  7. Article
  8. Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019
    Review
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

10 authors at 5 institutions in 1 country.

Akira KawanabeIntegrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University, Osaka, Japan.ORCID http://orcid.org/0000-0002-1094-6209
Masaki HashimotoGraduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Manami NishizawaSchool of Medical Technology, Teikyo University, Tokyo, Japan.
Kazuhisa NishizawaSchool of Medical Technology, Teikyo University, Tokyo, Japan.ORCID http://orcid.org/0000-0002-7642-6054
Hirotaka NaritaInstitute for Protein Research, Osaka University, Osaka, Japan.
Tomoko YonezawaIntegrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Yuka JinnoIntegrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University, Osaka, Japan.
Souhei SakataDepartment of Physiology, Division of Life Sciences, Faculty of Medicine, Osaka Medical College, Osaka, Japan.
Atsushi NakagawaInstitute for Protein Research, Osaka University, Osaka, Japan.ORCID http://orcid.org/0000-0002-1700-7861
Yasushi OkamuraIntegrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University, Osaka, Japan.ORCID http://orcid.org/0000-0001-5386-7968
The University of Osaka · JPProtein Research Foundation · JPTeikyo University · JPUbe Frontier University · JPOsaka Medical and Pharmaceutical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-sensing phosphatases (VSP) contain a voltage sensor domain (VSD) similar to that of voltage-gated ion channels but lack a pore-gate domain. A VSD in a VSP regulates the cytoplasmic catalytic region (CCR). However, the mechanisms by which the VSD couples to the CCR remain elusive. Here we report a membrane interface (named 'the hydrophobic spine'), which is essential for the coupling of the VSD and CCR. Our molecular dynamics simulations suggest that the hydrophobic spine of

Indexed as

Amino Acid SequenceAnimalsCatalytic DomainCiona intestinalisCytoplasmHydrophobic and Hydrophilic InteractionsIon Channel GatingMembranesMolecular Dynamics SimulationPhosphoric Monoester HydrolasesProtein DomainsPhosphoric Monoester HydrolasesascidianC. intestinalisdomain to domain couplingmembrane interactionmolecular biophysicsphosphatasephosphoinositidestructural biologyvoltage sensor

Identifiers

PMID30484774
PMCPMC6298786
OpenAlexW2902969533

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.