Evidence map›Paper›PMID 19419956›Full record

ArticleThe Journal of biological chemistry2009

Proliferating cell nuclear antigen is protected from degradation by forming a complex with MutT Homolog2.

Yu Yu, Jian-Ping Cai, Bo Tu, Lipeng Wu, Ying Zhao, Xiangyu Liu, Lian Li, Michael A McNutt, Jingnan Feng, Qihua He and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. 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
1.1field-weighted citation impact, top 23% 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, 52 citations in OpenAlex.

  1. Review
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  13. bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA).Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Review
  16. CREBBP and p300 lysine acetyl transferases in the DNA damage response.Cellular and molecular life sciences : CMLS · 2018
    Review
  17. Article
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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

14 authors at 4 institutions in 2 countries.

Yu YuKey Laboratory of Carcinogenesis and Translational Research (Education Ministry), Department of Biochemistry and Molecular Biology, Peking University Health Science Center, Beijing 100191, China.
Jian-Ping Cai
Bo Tu
Lipeng Wu
Ying Zhao
Xiangyu Liu
Lian Li
Michael A McNutt
Jingnan Feng
Qihua He
Yang Yang
Haiying Wang
Mutsuo Sekiguchi
Wei-Guo Zhu
Ministry of Education of the People's Republic of China · CNPeking University · CNFukuoka Dental College · JPNational Center for Clinical Laboratories · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proliferating cell nuclear antigen (PCNA) has been demonstrated to interact with multiple proteins involved in several metabolic pathways such as DNA replication and repair. However, there have been fewer reports about whether these PCNA-binding proteins influence stability of PCNA. Here, we observed a physical interaction between PCNA and MutT homolog2 (MTH2), a new member of the MutT-related proteins that hydrolyzes 8-oxo-7,8-dihydrodeoxyguanosine triphosphate (8-oxo-dGTP). In several unstressed human cancer cell lines and in normal human fibroblast cells, PCNA and MTH2 formed a complex and their mutual binding fragments were confirmed. It was intriguing that PCNA and MTH2 were dissociated dependent on acetylation of PCNA, which in turn induced degradation of PCNA in response to UV irradiation, but not in response to other forms of DNA-damaging stress. To further explore the link between dissociation of PCNA-MTH2 and degradation of PCNA, RNAi against MTH2 was performed to mimic the dissociated status of PCNA to evaluate changes in the half-life of PCNA. Knockdown of MTH2 significantly promoted degradation of PCNA, suggesting that the physiological interaction of PCNA-MTH2 may confer protection from degradation for PCNA, whereas UV irradiation accelerates PCNA degradation by inducing dissociation of PCNA-MTH2. Moreover, secondary to degradation of PCNA, UV-induced inhibition of DNA synthesis or cell cycle progression was enhanced. Collectively, our data demonstrate for the first time that PCNA is protected by this newly identified partner molecule MTH2, which is related to DNA synthesis and cell cycle progression.

Indexed as

AcetylationAzacitidineBlotting, WesternCell CycleCell LineCell Line, TumorDecitabineDeoxyguanine NucleotidesFluorescence Resonance Energy TransferHumansHydrogen PeroxideImmunoprecipitationLuminescent ProteinsMicroscopy, ConfocalNudix HydrolasesOxidants8-oxodeoxyguanosine triphosphateAzacitidineDecitabineDeoxyguanine NucleotidesHydrogen PeroxideLuminescent ProteinsNudix HydrolasesNUDT15 protein, humanOxidantsPhosphoric Diester HydrolasesProliferating Cell Nuclear AntigenPyrophosphatasesRecombinant Fusion ProteinsThymidine

Identifiers

PMID19419956
PMCPMC2740556
OpenAlexW2151896857

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.