Evidence map›Paper›PMID 31092600›Full record

ArticleThe Journal of biological chemistry2019

Prolyl hydroxylase 3 stabilizes the p53 tumor suppressor by inhibiting the p53-MDM2 interaction in a hydroxylase-independent manner.

Yiming Xu, Qiang Gao, Yaqian Xue, Xiuxiu Li, Liang Xu, Chenwei Li, Yanqing Qin, Jing Fang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  4. Proline hydroxylation of CREB-regulated transcriptional coactivator 2 controls hepatic glucose metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

8 authors at 3 institutions in 1 country.

Yiming XuFrom the Shanghai Institute for Nutrition and Health, Shanghai Institutes for Biological Sciences and.
Qiang GaoFrom the Shanghai Institute for Nutrition and Health, Shanghai Institutes for Biological Sciences and.
Yaqian XueFrom the Shanghai Institute for Nutrition and Health, Shanghai Institutes for Biological Sciences and.
Xiuxiu LiFrom the Shanghai Institute for Nutrition and Health, Shanghai Institutes for Biological Sciences and.
Liang Xuthe Institute for Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China.
Chenwei LiShanghai Sunstem Biotechnology, Shanghai 200437, China.
Yanqing QinFrom the Shanghai Institute for Nutrition and Health, Shanghai Institutes for Biological Sciences and.
Jing Fangthe Cancer Institute, Affiliated Hospital of Qingdao University, Qingdao 266061, China, and jfang@sibs.ac.cn.
Shanghai Institutes for Biological Sciences · CNAffiliated Hospital of Qingdao University · CNCenter for Excellence in Molecular Cell Science · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prolyl hydroxylase 3 (PHD3) has initially been reported to hydroxylase hypoxia-inducible factor α (HIFα) and mediate HIFα degradation. More recent studies have shown that, in addition to HIFα, PHD3 has also other substrates. Moreover, pHD3 is believed to act as a tumor suppressor, but the underlying mechanism remains to be elucidated. Here, we demonstrate that PHD3 stabilizes p53 in a hydroxylase-independent manner. We found that PHD3 overexpression increases and PHD3 knockdown decreases p53 levels. Mechanistically, PHD3 bound MDM2 proto-oncogene (MDM2) and prevented MDM2 from interacting with p53, thereby inhibiting MDM2-mediated p53 degradation. Interestingly, we found that PHD3 overexpression could enhance p53 in the presence of the prolyl hydroxylase inhibitor dimethyloxalylglycine, and the prolyl hydroxylase activity-deficient variant PHD3-H196A also inhibited the p53-MDM2 interaction and stabilized p53. Genetic ablation of PHD3 decreased p53 protein levels in mice intestinal epithelial cells, but a genetic knockin of PHD3-H196A did not affect p53 protein levels

Indexed as

AnimalsColonic NeoplasmsHumansHypoxia-Inducible Factor-Proline DioxygenasesMiceMice, Inbred C57BLMice, KnockoutNeoplastic Stem CellsProcollagen-Proline DioxygenaseProto-Oncogene MasProto-Oncogene Proteins c-mdm2Tumor Cells, CulturedTumor Suppressor Protein p53UbiquitinationEGLN3 protein, humanHypoxia-Inducible Factor-Proline DioxygenasesMAS1 protein, humanMDM2 protein, humanPHD3 protein, mouseProcollagen-Proline DioxygenaseProto-Oncogene MasProto-Oncogene Proteins c-mdm2TP53 protein, humanTumor Suppressor Protein p53cancer stem cellscolon cancermouse double minute 2 homolog (MDM2)p53prolyl hydroxylase 3protein stability

Identifiers

PMID31092600
PMCPMC6597825
OpenAlexW2946044809

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.