Evidence map›Paper›PMID 32214225›Full record

ArticleCommunications biology2020

The Na,K-ATPase acts upstream of phosphoinositide PI(4,5)P

Cyril Legrand, Roberto Saleppico, Jana Sticht, Fabio Lolicato, Hans-Michael Müller, Sabine Wegehingel, Eleni Dimou, Julia P Steringer, Helge Ewers, Ilpo Vattulainen and 2 more

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Communications biology, 2020. 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
1.8field-weighted citation impact, top 14% 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, 33 citations in OpenAlex.

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  14. Unconventional Pathways of Protein Secretion: MammalsFrontiers in cell and developmental biology · 2022
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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 3 institutions in 2 countries.

Cyril Legrand *Heidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-0134-4166
Roberto Saleppico *Heidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-0502-192X
Jana StichtInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, 14195, Berlin, Germany.
Fabio LolicatoHeidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.
Hans-Michael MüllerHeidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-2384-7285
Sabine WegehingelHeidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.
Eleni DimouHeidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-4885-135X
Julia P SteringerHeidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany.
Helge EwersInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, 14195, Berlin, Germany.ORCID http://orcid.org/0000-0003-3948-4332
Ilpo VattulainenDepartment of Physics, University of Helsinki, FL-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0001-7408-3214
Christian FreundInstitute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, 14195, Berlin, Germany.
Walter NickelHeidelberg University Biochemistry Center, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany. walter.nickel@bzh.uni-heidelberg.de.ORCID http://orcid.org/0000-0002-6496-8286
Heidelberg University · DEFreie Universität Berlin · DEUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FGF2 is a tumor cell survival factor that is exported from cells by an ER/Golgi-independent secretory pathway. This unconventional mechanism of protein secretion is based on direct translocation of FGF2 across the plasma membrane. The Na,K-ATPase has previously been shown to play a role in this process, however, the underlying mechanism has remained elusive. Here, we define structural elements that are critical for a direct physical interaction between FGF2 and the α1 subunit of the Na,K-ATPase. In intact cells, corresponding FGF2 mutant forms were impaired regarding both recruitment at the inner plasma membrane leaflet and secretion. Ouabain, a drug that inhibits both the Na,K-ATPase and FGF2 secretion, was found to impair the interaction of FGF2 with the Na,K-ATPase in cells. Our findings reveal the Na,K-ATPase as the initial recruitment factor for FGF2 at the inner plasma membrane leaflet being required for efficient membrane translocation of FGF2 to cell surfaces.

Indexed as

AnimalsCell MembraneCHO CellsCricetulusFibroblast Growth Factor 2Molecular Docking SimulationMolecular Dynamics SimulationPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein Interaction Domains and MotifsProtein TransportSecond Messenger SystemsSecretory PathwaySodium-Potassium-Exchanging ATPaseATP1A1 protein, humanFibroblast Growth Factor 2Phosphatidylinositol 4,5-DiphosphateSodium-Potassium-Exchanging ATPase

Identifiers

PMID32214225
PMCPMC7096399
OpenAlexW3013112074

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.