Evidence map›Paper›PMID 26055329›Full record

ArticleMolecular and cellular biology2015

TRIM28 Is an E3 Ligase for ARF-Mediated NPM1/B23 SUMOylation That Represses Centrosome Amplification.

Shu Hui Neo, Yoko Itahana, Jennifer Alagu, Mayumi Kitagawa, Alvin Kunyao Guo, Sang Hyun Lee, Kai Tang, Koji Itahana

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

31 citing papers in PubMed, 45 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. Mutant p53Molecular oncology · 2026
    Article
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  20. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
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

8 authors at 3 institutions in 1 country.

Shu Hui NeoCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore.
Yoko ItahanaCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore.
Jennifer AlaguCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore.
Mayumi KitagawaCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore.
Alvin Kunyao GuoCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore.
Sang Hyun LeeCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore.
Kai TangDivision of Structural Biology Biochemistry, School of Biological Sciences, College of Science, Nanyang Technological University, Singapore, Singapore.
Koji ItahanaCancer & Stem Cell Biology Program, Duke-NUS Graduate Medical School Singapore, Singapore, Singapore koji.itahana@duke-nus.edu.sg.
Duke-NUS Medical School · SGNational University of Singapore · SGNanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumor suppressor ARF enhances the SUMOylation of target proteins; however, the physiological function of ARF-mediated SUMOylation has been unclear due to the lack of a known, associated E3 SUMO ligase. Here we uncover TRIM28/KAP1 as a novel ARF-binding protein and SUMO E3 ligase for NPM1/B23. ARF and TRIM28 cooperate to SUMOylate NPM1, a nucleolar protein that regulates centrosome duplication and genomic stability. ARF-mediated SUMOylation of NPM1 was attenuated by TRIM28 depletion and enhanced by TRIM28 overexpression. Coexpression of ARF and TRIM28 promoted NPM1 centrosomal localization by enhancing its SUMOylation and suppressed centrosome amplification; these functions required the E3 ligase activity of TRIM28. Conversely, depletion of ARF or TRIM28 increased centrosome amplification. ARF also counteracted oncogenic Ras-induced centrosome amplification. Centrosome amplification is often induced by oncogenic insults, leading to genomic instability. However, the mechanisms employed by tumor suppressors to protect the genome are poorly understood. Our findings suggest a novel role for ARF in maintaining genome integrity by facilitating TRIM28-mediated SUMOylation of NPM1, thus preventing centrosome amplification.

Indexed as

ADP-Ribosylation FactorsAnimalsCell Line, TumorCentrosomeHumansMiceNIH 3T3 CellsNuclear ProteinsNucleophosminProtein Interaction MapsRepressor ProteinsSumoylationTripartite Motif-Containing Protein 28Ubiquitin-Protein LigasesADP-Ribosylation FactorsNPM1 protein, humanNpm1 protein, mouseNuclear ProteinsNucleophosminRepressor ProteinsTRIM28 protein, humanTripartite Motif-Containing Protein 28Ubiquitin-Protein Ligases

Identifiers

PMID26055329
PMCPMC4508312
OpenAlexW2101281806

What OpenQuestion holds

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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.