Evidence map›Paper›PMID 22896666›Full record

ArticleJournal of lipid research2012

A human phospholipid phosphatase activated by a transmembrane control module.

Christian R Halaszovich, Michael G Leitner, Angeliki Mavrantoni, Audrey Le, Ludivine Frezza, Anja Feuer, Daniela N Schreiber, Carlos A Villalba-Galea, Dominik Oliver

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  4. Predicting the Structural Impact of Human Alternative Splicing.bioRxiv : the preprint server for biology · 2023
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  8. Modulation of KFrontiers in pharmacology · 2020
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  10. OverexpressingOncotarget · 2018
    Article
  11. KChannels (Austin, Tex.) · 2018
    Article
  12. Review
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  14. Discovery and functional characterization of a neomorphic PTEN mutation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Review
  17. Article
  18. Voltage-Controlled Enzymes: The New JanusBifrons.Frontiers in pharmacology · 2012
    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

9 authors at 3 institutions in 2 countries.

Christian R HalaszovichInstitute of Physiology and Pathophysiology, Philipps-Universität Marburg, 35037 Marburg, Germany.
Michael G Leitner
Angeliki Mavrantoni
Audrey Le
Ludivine Frezza
Anja Feuer
Daniela N Schreiber
Carlos A Villalba-Galea
Dominik Oliver
Philipps University of Marburg · DEVirginia Commonwealth University · USUniversity of Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In voltage-sensitive phosphatases (VSPs), a transmembrane voltage sensor domain (VSD) controls an intracellular phosphoinositide phosphatase domain, thereby enabling immediate initiation of intracellular signals by membrane depolarization. The existence of such a mechanism in mammals has remained elusive, despite the presence of VSP-homologous proteins in mammalian cells, in particular in sperm precursor cells. Here we demonstrate activation of a human VSP (hVSP1/TPIP) by an intramolecular switch. By engineering a chimeric hVSP1 with enhanced plasma membrane targeting containing the VSD of a prototypic invertebrate VSP, we show that hVSP1 is a phosphoinositide-5-phosphatase whose predominant substrate is PI(4,5)P(2). In the chimera, enzymatic activity is controlled by membrane potential via hVSP1's endogenous phosphoinositide binding motif. These findings suggest that the endogenous VSD of hVSP1 is a control module that initiates signaling through the phosphatase domain and indicate a role for VSP-mediated phosphoinositide signaling in mammals.

Indexed as

AnimalsCHO CellsCricetinaeElectrophysiologyHumansMicroscopy, FluorescenceOocytesPhosphatidylinositolsPhosphoric Monoester HydrolasesSignal TransductionXenopusPhosphatidylinositolsPhosphoric Monoester Hydrolases

Identifiers

PMID22896666
PMCPMC3465996
OpenAlexW2161033576

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.