Evidence map›Paper›PMID 29283500›Full record

ArticleThe FEBS journal2018

Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf.

Enrico Luchinat, Sara Chiarella, Mimma Franceschini, Adele Di Matteo, Maurizio Brunori, Lucia Banci, Luca Federici

Open access · bronzeAbstract readComparative Study
PubMed Publisher
In one paragraph

Article in The FEBS journal, 2018. 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
2.0field-weighted citation impact, top 12% 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, 23 citations in OpenAlex.

  1. Tyrosine phosphorylation unfolds nucleophosmin and disrupts its integration into the nucleolus.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Review
  4. p14Nature communications · 2024
    Article
  5. Article
  6. Review
  7. p14Research square · 2023
    Article
  8. Article
  9. Article
  10. Jab1 promotes gastric cancer tumorigenesis via non-ubiquitin proteasomal degradation of p14ARF.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2020
    Article
  11. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    Review
  12. Nucleophosmin in Its Interaction with Ligands.International journal of molecular sciences · 2020
    Review
  13. The Dundee Resource for Sequence Analysis and Structure Prediction.Protein science : a publication of the Protein Society · 2020
    Article
  14. Review
  15. The nucleolus, an ally, and an enemy of cancer cells.Histochemistry and cell biology · 2018
    Review
  16. Review
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 1 country.

Enrico LuchinatCERM, Centro Risonanze Magnetiche, Università di Firenze, Italy.
Sara ChiarellaCe.S.I.-MeT Centro di Scienze dell'Invecchiamento e Medicina Traslazionale, Università "G. d'Annunzio" di Chieti, Italy.
Mimma FranceschiniCe.S.I.-MeT Centro di Scienze dell'Invecchiamento e Medicina Traslazionale, Università "G. d'Annunzio" di Chieti, Italy.
Adele Di MatteoIstituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy.
Maurizio BrunoriDipartimento di Scienze Biochimiche, "A. Rossi Fanelli" - Sapienza Università di Roma, Italy.
Lucia BanciCERM, Centro Risonanze Magnetiche, Università di Firenze, Italy.
Luca FedericiCe.S.I.-MeT Centro di Scienze dell'Invecchiamento e Medicina Traslazionale, Università "G. d'Annunzio" di Chieti, Italy.
University of Chieti-Pescara · ITInstitute of Molecular Biology and Pathology · ITInteruniversity Consortium for Magnetic Resonance · ITSapienza University of Rome · ITUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumor suppressor p14arf interacts, in response to oncogenic signals, with the p53 E3-ubiquitin ligase HDM2, thereby resulting in p53 stabilization and activation. In addition, it also exerts tumor-suppressive functions in p53-independent contexts. The activities of p14arf are regulated by the nucleolar chaperone nucleophosmin (NPM1), which controls its levels and cellular localization. In acute myeloid leukemia with mutations in the NPM1 gene, mutated NPM1 aberrantly translocates in the cytosol carrying with itself p14arf that is subsequently degraded, thus impairing the p14arf-HDM2-p53 axis. In this work we investigated the complex between these two proteins by means of NMR and other techniques. We identified a novel NPM1-interacting motif in the C-terminal region of p14arf, which corresponds to its predicted nucleolar localization signal. This motif recognizes a specific region of the NPM1 N-terminal domain and, upon binding, the two proteins form soluble high molecular weight complexes. By NMR, we identified critical residues on both proteins involved in the interaction. Collectively, our data provide a structural framework to rationalize the overall assembly of the p14arf-NPM1 supramolecular complexes. A number of p14arf cancer-associated mutations cluster in this motif and their effect on the interaction with NPM1 was also analyzed.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsHumansLeukemia, Myeloid, AcuteMiceModels, MolecularMolecular Targeted TherapyMutationNeoplasm ProteinsNeoplasmsNuclear Magnetic Resonance, BiomolecularNuclear ProteinsNucleophosminProtein AggregatesProtein ConformationNeoplasm ProteinsNPM1 protein, humanNpm1 protein, mouseNuclear ProteinsNucleophosminProtein AggregatesRecombinant Fusion ProteinsTumor Suppressor Protein p14ARFacute myeloid leukemiaARFB23cancer targetNPM1protein-protein interactions

Identifiers

PMID29283500
OpenAlexW2781221303

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.