Evidence map›Paper›PMID 24277865›Full record

ArticleThe Journal of physiology2014

Phosphatase activity of the voltage-sensing phosphatase, VSP, shows graded dependence on the extent of activation of the voltage sensor.

Souhei Sakata, Yasushi Okamura

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Heat- and PIP2-dependent TRPM4 activity underlies mutually exclusive human diseases.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Voltage sensors.Molecular pharmacology · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Mechanism of voltage gating in the voltage-sensing phosphatase Ci-VSP.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Engineering an enhanced voltage-sensing phosphatase.The Journal of general physiology · 2020
    Article
  9. Article
  10. 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
  11. Review
  12. Article
  13. Article
  14. Review
  15. Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Simple scheme of lipid enzyme can explain complex lives of phosphoinositides.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Souhei SakataLaboratory of Integrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University, 2-2 Yamada-Oka, Suita, Osaka 565-0871, Japan.  sakata@phys2.med.osaka-u.ac.jp.
Yasushi Okamura
Community Initiatives · USOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The voltage-sensing phosphatase (VSP) consists of a voltage sensor and a cytoplasmic phosphatase region, and the movement of the voltage sensor is coupled to the phosphatase activity. However, its coupling mechanisms still remain unclear. One possible scenario is that the phosphatase is activated only when the voltage sensor is in a fully activated state. Alternatively, the enzymatic activity of single VSP proteins could be graded in distinct activated states of the voltage sensor, and partial activation of the voltage sensor could lead to partial activation of the phosphatase. To distinguish between these two possibilities, we studied a voltage sensor mutant of zebrafish VSP, where the voltage sensor moves in two steps as evidenced by analyses of charge movements of the voltage sensor and voltage clamp fluorometry. Measurements of the phosphatase activity toward phosphatidylinositol 4,5-bisphosphate revealed that both steps of voltage sensor activation are coupled to the tuning of phosphatase activities, consistent with the idea that the phosphatase activity is graded by the magnitude of the movement of the voltage sensor.

Indexed as

AnimalsCell MembraneCells, CulturedEnzyme ActivationIon Channel GatingMembrane PotentialsMotionOocytesPhosphoric Monoester HydrolasesXenopus laevisZebrafish ProteinsPhosphoric Monoester Hydrolasestpte protein, zebrafishZebrafish Proteins

Identifiers

PMID24277865
PMCPMC3948554
OpenAlexW1608751979

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.