Evidence map›Paper›PMID 28302728›Full record

ArticleThe Journal of biological chemistry2017

High phosphatidylinositol 4-phosphate (PI4P)-dependent ATPase activity for the Drs2p-Cdc50p flippase after removal of its N- and C-terminal extensions.

Hassina Azouaoui, Cédric Montigny, Thibaud Dieudonné, Philippe Champeil, Aurore Jacquot, José Luis Vázquez-Ibar, Pierre Le Maréchal, Jakob Ulstrup, Miriam-Rose Ash, Joseph A Lyons and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Flippase-Mediated Hybrid Vesicle Division.Advanced materials (Deerfield Beach, Fla.) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Functional Analysis of the P-Type ATPases Apt2-4 fromJournal of fungi (Basel, Switzerland) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. 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

12 authors at 2 institutions in 2 countries.

Hassina AzouaouiFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
Cédric MontignyFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
Thibaud DieudonnéFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
Philippe ChampeilFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
Aurore JacquotFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
José Luis Vázquez-IbarFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
Pierre Le Maréchalthe Neuro-PSI-UMR CNRS 9197, Bâtiment 430, Université Paris-Sud, Université Paris-Saclay, 91405 Orsay Cedex, France, and.
Jakob Ulstrupthe DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, and PUMPkin, Department of Molecular Biology and Genetics, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark.
Miriam-Rose Ashthe DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, and PUMPkin, Department of Molecular Biology and Genetics, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark.ORCID 0000-0002-0573-9854
Joseph A Lyonsthe DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, and PUMPkin, Department of Molecular Biology and Genetics, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark.
Poul Nissenthe DANDRITE, Nordic-EMBL Partnership for Molecular Medicine, and PUMPkin, Department of Molecular Biology and Genetics, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark.ORCID 0000-0003-0948-6628
Guillaume LenoirFrom the Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France, guillaume.lenoir@i2bc.paris-saclay.fr.ORCID 0000-0002-8759-5179
Université Paris-Sud · FRDanish National Research Foundation · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P4-ATPases, also known as phospholipid flippases, are responsible for creating and maintaining transbilayer lipid asymmetry in eukaryotic cell membranes. Here, we use limited proteolysis to investigate the role of the N and C termini in ATP hydrolysis and auto-inhibition of the yeast flippase Drs2p-Cdc50p. We show that limited proteolysis of the detergent-solubilized and purified yeast flippase may result in more than 1 order of magnitude increase of its ATPase activity, which remains dependent on phosphatidylinositol 4-phosphate (PI4P), a regulator of this lipid flippase, and specific to a phosphatidylserine substrate. Using thrombin as the protease, Cdc50p remains intact and in complex with Drs2p, which is cleaved at two positions, namely after Arg

Indexed as

Adenosine TriphosphateArginineCalcium-Transporting ATPasesHydrolysisMutationPhosphatidylinositol PhosphatesPhospholipidsPhospholipid Transfer ProteinsPhosphorylationProtein BindingProtein DomainsProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThrombinAdenosine TriphosphateArginineCalcium-Transporting ATPasesCDC50 protein, S cerevisiaeDRS2 protein, S cerevisiaephosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhospholipidsPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsThrombinautophosphorylationCDC50 proteinflippaseinhibition mechanismlimited proteolysislipid-protein interactionphosphatidylserinephosphoinositide

Identifiers

PMID28302728
PMCPMC5427273
OpenAlexW2595577396

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.