Evidence map›Paper›PMID 28493957›Full record

ArticlePloS one2017

Ezrin interacts with S100A4 via both its N- and C-terminal domains.

Beáta Biri-Kovács, Bence Kiss, Henrietta Vadászi, Gergő Gógl, Gyula Pálfy, György Török, László Homolya, Andrea Bodor, László Nyitray

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Tumor-Suppressor p53TADChembiochem : a European journal of chemical biology · 2020
    Article
  11. Article
  12. S-Nitrosylation: An Emerging Paradigm of Redox Signaling.Antioxidants (Basel, Switzerland) · 2019
    Review
  13. Article
  14. Review
  15. Detecting the location and significance of Ezrin protein expression in hepatocellular carcinoma.International journal of clinical and experimental pathology · 2018
    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 2 institutions in 1 country.

Beáta Biri-KovácsDepartment of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Bence KissDepartment of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Henrietta VadásziDepartment of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Gergő GóglDepartment of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Gyula PálfyInstitute of Chemistry, Laboratory of Structural Chemistry and Biology, Eötvös Loránd University, Budapest, Hungary.
György TörökMolecular Cell Biology Research Group, Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary.
László HomolyaMolecular Cell Biology Research Group, Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary.
Andrea BodorInstitute of Chemistry, Laboratory of Structural Chemistry and Biology, Eötvös Loránd University, Budapest, Hungary.
László NyitrayDepartment of Biochemistry, Eötvös Loránd University, Budapest, Hungary.ORCID http://orcid.org/0000-0003-4717-5994
Eötvös Loránd University · HUInstitute of Molecular Life Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ezrin belongs to the ERM (ezrin, radixin, moesin) protein family that has a role in cell morphology changes, adhesion and migration as an organizer of the cortical cytoskeleton by linking actin filaments to the apical membrane of epithelial cells. It is highly expressed in a variety of human cancers and promotes metastasis. Members of the Ca2+-binding EF-hand containing S100 proteins have similar pathological properties; they are overexpressed in cancer cells and involved in metastatic processes. In this study, using tryptophan fluorescence and stopped-flow kinetics, we show that S100A4 binds to the N-terminal ERM domain (N-ERMAD) of ezrin with a micromolar affinity. The binding involves the F2 lobe of the N-ERMAD and follows an induced fit kinetic mechanism. Interestingly, S100A4 binds also to the unstructured C-terminal actin binding domain (C-ERMAD) with similar affinity. Using NMR spectroscopy, we characterized the complex of S100A4 with the C-ERMAD and demonstrate that no ternary complex is simultaneously formed with the two ezrin domains. Furthermore, we show that S100A4 co-localizes with ezrin in HEK-293T cells. However, S100A4 very weakly binds to full-length ezrin in vitro indicating that the interaction of S100A4 with ezrin requires other regulatory events such as protein phosphorylation and/or membrane binding, shifting the conformational equilibrium of ezrin towards the open state. As both proteins play an important role in promoting metastasis, the characterization of their interaction could shed more light on the molecular events contributing to this pathological process.

Indexed as

Cell LineCircular DichroismCytoskeletal ProteinsEzrinHumansMagnetic Resonance SpectroscopyPhosphorylationProtein BindingProtein DomainsS100 Calcium-Binding Protein A4TryptophanCytoskeletal ProteinsEzrinS100 Calcium-Binding Protein A4Tryptophan

Identifiers

PMID28493957
PMCPMC5426754
OpenAlexW2613275228

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.