Evidence map›Paper›PMID 26238070›Full record

ArticleScientific reports2015

HAUSP-nucleolin interaction is regulated by p53-Mdm2 complex in response to DNA damage response.

Key-Hwan Lim, Jang-Joon Park, Bon-Hee Gu, Jin-Ock Kim, Sang Gyu Park, Kwang-Hyun Baek

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. 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 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, 36 citations in OpenAlex.

  1. Review
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  5. Dual Aptamers-Based SETDB1 PROTACs as Effective Anti-Tumor Strategies for Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  7. VpdC is a ubiquitin-activated phospholipase effector that regulatesProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. Review
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  14. Article
  15. The Nucleolus: In Genome Maintenance and Repair.International journal of molecular sciences · 2017
    Review
  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

6 authors at 2 institutions in 1 country.

Key-Hwan LimDepartment of Biomedical Science, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea.
Jang-Joon ParkDepartment of Biomedical Science, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea.
Bon-Hee GuDepartment of Biomedical Science, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea.
Jin-Ock KimDepartment of Biomedical Science, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea.
Sang Gyu ParkCollege of Pharmacy, Ajou University, Suwon, Gyeonggi-Do 443-749, Republic of Korea.
Kwang-Hyun BaekDepartment of Biomedical Science, CHA University, Bundang CHA General Hospital, Gyeonggi-Do 463-400, Republic of Korea.
CHA University · KRAjou University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HAUSP (herpes virus-associated ubiquitin specific protease, known as ubiquitin specific protease 7), one of DUBs, regulates the dynamics of the p53 and Mdm2 network in response to DNA damage by deubiquitinating both p53 and its E3 ubiquitin ligase, Mdm2. Its concerted action increases the level of functional p53 by preventing proteasome-dependent degradation of p53. However, the protein substrates that are targeted by HAUSP to mediate DNA damage responses in the context of the HAUSP-p53-Mdm2 complex are not fully identified. Here, we identified nucleolin as a new substrate for HAUSP by proteomic analysis. Nucleolin has two HAUSP binding sites in its N- and C-terminal regions, and the mutation of HAUSP interacting peptides on nucleolin disrupts their interaction and it leads to the increased level of nucleolin ubiquitination. In addition, HAUSP regulates the stability of nucleolin by removing ubiquitin from nucleolin. Nucleolin exists as a component of the HAUSP-p53-Mdm2 complex, and both Mdm2 and p53 are required for the interaction between HAUSP and nucleolin. Importantly, the irradiation increases the HAUSP-nucleolin interaction, leading to nucleolin stabilization significantly. Taken together, this study reveals a new component of the HAUSP-p53-Mdm2 complex that governs dynamic cellular responses to DNA damage.

Indexed as

Annexin A1DNA DamageGene Expression RegulationHCT116 CellsHEK293 CellsHeLa CellsHumansMCF-7 CellsNucleolinPhosphoproteinsProteasome Endopeptidase ComplexProtein StabilityProteolysisProto-Oncogene Proteins c-mdm2RNA-Binding ProteinsRNA, Small InterferingAnnexin A1MDM2 protein, humanNucleolinPhosphoproteinsProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mdm2RNA-Binding ProteinsRNA, Small InterferingTumor Suppressor Protein p53UbiquitinUbiquitin-Specific Peptidase 7Ubiquitin ThiolesteraseUSP7 protein, human

Identifiers

PMID26238070
PMCPMC4523935
OpenAlexW1057963698

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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.