Evidence map›Paper›PMID 38664499›Full record

ArticleOncogene2024

Non-canonical deubiquitination of OTUB1 induces IFNγ-mediated cell cycle arrest via regulation of p27 stability.

Seul Gi Lee, Seon Min Woo, Seung Un Seo, Hyun Shik Lee, Sang Hyun Kim, Young-Chae Chang, Hyo Je Cho, Simmyung Yook, Ju-Ock Nam, Taeg Kyu Kwon

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Oncogene, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Selective Modulation of OTUB1 Noncanonical Function via a bioPhosTAC Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Review
  4. Review
  5. 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

10 authors at 6 institutions in 2 countries.

Seul Gi LeeDepartment of Immunology, School of Medicine, Keimyung University, Daegu, 42601, South Korea.ORCID 0000-0001-8186-0886
Seon Min WooDepartment of Immunology, School of Medicine, Keimyung University, Daegu, 42601, South Korea.ORCID 0000-0003-4963-9895
Seung Un SeoDepartment of Immunology, School of Medicine, Keimyung University, Daegu, 42601, South Korea.
Hyun Shik LeeSchool of Life Sciences, BK21 Plus KNU Creative BioResearch Group, College of Natural Sciences, Kyungpook National University, Daegu, 41566, South Korea.ORCID 0000-0002-3837-9867
Sang Hyun KimDepartment of Pharmacology, School of Medicine, Kyungpook National University, Daegu, 41944, South Korea.
Young-Chae ChangResearch Institute of Biomedical Engineering and Department of Medicine, Catholic University of Daegu School of Medicine, Daegu, 42472, South Korea.ORCID 0000-0003-2667-7303
Hyo Je ChoDepartment of Biochemistry, Chungbuk National University, Cheongju, 28644, South Korea.
Simmyung YookDepartment of Biopharmaceutical Convergence, Sungkyunkwan University, Suwon, 16419, South Korea.
Ju-Ock NamDepartment of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, South Korea.
Taeg Kyu KwonDepartment of Immunology, School of Medicine, Keimyung University, Daegu, 42601, South Korea. kwontk@dsmc.or.kr.ORCID 0000-0003-1204-2059
Keimyung University · KRKyungpook National University · KRChungbuk National University · KRDaegu Catholic University · KRSungkyunkwan University · KRUniversity of Virginia · US

Funding

National Research Foundation of Korea (NRF) NRF-2019R1A2C2005921National Research Foundation of Korea (NRF) NRF-2021R1A4A1029238National Research Foundation of Korea (NRF) RS-2023-00211824
6 · The paper itself

Abstract

The deubiquitinase OTUB1, implicated as a potential oncogene in various tumors, lacks clarity in its regulatory mechanism in tumor progression. Our study investigated the effects and underlying mechanisms of OTUB1 on the breast cancer cell cycle and proliferation in IFNγ stimulation. Loss of OTUB1 abrogated IFNγ-induced cell cycle arrest by regulating p27 protein expression, whereas OTUB1 overexpression significantly enhanced p27 expression even without IFNγ treatment. Tyr26 phosphorylation residue of OTUB1 directly bound to p27, modulating its post-translational expression. Furthermore, we identified crucial lysine residues (K134, K153, and K163) for p27 ubiquitination. Src downregulation reduced OTUB1 and p27 expression, suggesting that IFNγ-induced cell cycle arrest is mediated by the Src-OTUB1-p27 signaling pathway. Our findings highlight the pivotal role of OTUB1 in IFNγ-induced p27 expression and cell cycle arrest, offering therapeutic implications.

Indexed as

Cell Cycle CheckpointsCyclin-Dependent Kinase Inhibitor p27Deubiquitinating EnzymesInterferon-gammaUbiquitinationBreast NeoplasmsCell Line, TumorCell ProliferationCysteine EndopeptidasesFemaleHumansPhosphorylationProtein StabilitySignal TransductionCyclin-Dependent Kinase Inhibitor p27Cysteine EndopeptidasesDeubiquitinating EnzymesInterferon-gammaOTUB1 protein, human

Identifiers

PMID38664499
PMCPMC11164677
OpenAlexW4395456063

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.