Evidence map›Paper›PMID 26077467›Full record

ArticleNature communications2015

Programmed cell death 5 mediates HDAC3 decay to promote genotoxic stress response.

Hyo-Kyoung Choi, Youngsok Choi, Eun Sung Park, Soo-Yeon Park, Seung-Hyun Lee, Jaesung Seo, Mi-Hyeon Jeong, Jae-Wook Jeong, Jae-Ho Jeong, Peter C W Lee and 2 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 58 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 2 countries.

Hyo-Kyoung ChoiDepartment of Biochemistry and Molecular Biology, Brain Korea 21 PLUS Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Youngsok ChoiDepartment of Biomedical Science, CHA University, 335 Pangyo-ro, Bundang-gu, Seongnam-si, Gyeonggi-do 436-400, Korea.
Eun Sung ParkMedical Convergence Research Institute, Yonsei University College of Medicine, Seoul 120-752, Korea.
Soo-Yeon ParkDepartment of Biochemistry and Molecular Biology, Brain Korea 21 PLUS Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Seung-Hyun LeeDepartment of Biochemistry and Molecular Biology, Brain Korea 21 PLUS Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Jaesung SeoDepartment of Biochemistry and Molecular Biology, Brain Korea 21 PLUS Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Mi-Hyeon JeongDepartment of Biochemistry and Molecular Biology, Brain Korea 21 PLUS Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Jae-Wook JeongDepartment of Obstetrics, Gynecology and Reproductive Biology, Michigan State University College of Human Medicine, Lansing, Michigan 49503, USA.
Jae-Ho JeongDepartment of Surgery, Yonsei University College of Medicine, Seoul 120-752, Korea.
Peter C W LeeDepartment of Biomedical Sciences, University of Ulsan College of Medicine, Seoul 138-736, Korea.
Kyung-Chul ChoiDepartment of Biomedical Sciences, University of Ulsan College of Medicine, Seoul 138-736, Korea.
Ho-Geun YoonDepartment of Biochemistry and Molecular Biology, Brain Korea 21 PLUS Project for Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Yonsei University · KRCHA University · KRMichigan State University · USUlsan College · KRUniversity of Ulsan · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inhibition of p53 activity by histone deacetylase 3 (HDAC3) has been reported, but the precise molecular mechanism is unknown. Here we show that programmed cell death 5 (PDCD5) selectively mediates HDAC3 dissociation from p53, which induces HDAC3 cleavage and ubiquitin-dependent proteasomal degradation. Casein kinase 2 alpha phosphorylates PDCD5 at Ser-119 to enhance its stability and importin 13-mediated nuclear translocation of PDCD5. Genetic deletion of PDCD5 abrogates etoposide (ET)-induced p53 stabilization and HDAC3 cleavage, indicating an essential role of PDCD5 in p53 activation. Restoration of PDCD5(WT) in PDCD5(-/-) MEFs restores ET-induced HDAC3 cleavage. Reduction of both PDCD5 and p53, but not reduction of either protein alone, significantly enhances in vivo tumorigenicity of AGS gastric cancer cells and correlates with poor prognosis in gastric cancer patients. Our results define a mechanism for p53 activation via PDCD5-dependent HDAC3 decay under genotoxic stress conditions.

Indexed as

AnimalsApoptosis Regulatory ProteinsCasein Kinase IICell Line, TumorChromatin ImmunoprecipitationDNA DamageFibroblastsGene Expression ProfilingHCT116 CellsHistone Deacetylase 3Histone DeacetylasesHumansImmunoprecipitationIn Situ Nick-End LabelingKaryopherinsMass SpectrometryApoptosis Regulatory ProteinsCasein Kinase IIHistone Deacetylase 3Histone Deacetylasesimportin 13 protein, mouseIPO13 protein, humanKaryopherinsNeoplasm ProteinsPDCD5 protein, humanPdcd5 protein, mouseProteasome Endopeptidase ComplexTumor Suppressor Protein p53

Identifiers

PMID26077467
PMCPMC4490383
OpenAlexW2196487903

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.