Evidence map›Paper›PMID 34362424›Full record

ArticleJournal of experimental & clinical cancer research : CR2021

Ribosomal L1 domain-containing protein 1 coordinates with HDM2 to negatively regulate p53 in human colorectal Cancer cells.

Li Ding, Zhiping Zhang, Chenhong Zhao, Lei Chen, Zhiqiang Chen, Jie Zhang, Yaxian Liu, Yesen Nie, Yanzhi He, Kai Liao and 1 more

Open access · goldAbstract read
In one paragraph

Article in Journal of experimental & clinical cancer research : CR, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-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

9 citing papers in PubMed, 15 citations in OpenAlex.

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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

11 authors at 2 institutions in 1 country.

Li DingCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Zhiping ZhangCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Chenhong ZhaoCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Lei ChenCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Zhiqiang ChenCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Jie ZhangCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Yaxian LiuCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Yesen NieCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Yanzhi HeCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Kai LiaoCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China.
Xinyue ZhangCollege of Bioscience and Biotechnology, Yangzhou University, Yangzhou, 225009, Jiangsu, China. zhanglabsubmission@163.com.
Yangzhou University · CNJiangsu Provincial Center for Disease Control and Prevention · CN

Funding

Natural Science Foundation of China for Young Scientists 81802765Natural Science Foundation of Jiangsu Province for Young Scientists BK20160478Postdoctoral Research Funding Plan of Jiangsu Province 1601041Bpostgraduate research & practice innovation program of jiangsu province KYCX21_3206Scientific and Technological Innovation Fostering Foundation of Yangzhou University 2016CXJ090Six Talent Peaks Project in Jiangsu Province 2014-SWYY-016
6 · The paper itself

Abstract

backgroundRibosomal L1 domain-containing protein 1 (RSL1D1) is a nucleolar protein that is essential in cell proliferation. In the current opinion, RSL1D1 translocates to the nucleoplasm under nucleolar stress and inhibits the E3 ligase activity of HDM2 via direct interaction, thereby leading to stabilization of p53.

methodsGene knockdown was achieved in HCT116

resultsRSL1D1 distributed throughout the nucleus in human CRC cells. Silencing of RSL1D1 gene induced cell cycle arrest at G1/S and cell apoptosis in a p53-dependent manner. RSL1D1 directly interacted with and recruited p53 to HDM2 to form a ternary RSL1D1/HDM2/p53 protein complex and thereby enhanced p53 ubiquitination and degradation, leading to a decrease in the protein level of p53. Destruction of the ternary complex increased the level of p53 protein. RSL1D1 also indirectly decreased the protein level of p53 by stabilizing HDM2 mRNA. Consequently, the negative regulation of p53 by RSL1D1 facilitated cell proliferation and survival and downregulation of RSL1D1 remarkably inhibited the growth of HCT116

conclusionWe report, for the first time, that RSL1D1 is a novel negative regulator of p53 in human CRC cells and more importantly, a potential molecular target for anticancer drug development.

Indexed as

AnimalsColorectal NeoplasmsDisease Models, AnimalFemaleGene Knockdown TechniquesHCT116 CellsHeterograftsHumansMiceMice, Inbred BALB CMice, NudePregnancy ProteinsProto-Oncogene Proteins c-mdm2Ribosomal ProteinsTransfectionTumor Suppressor Protein p53MDM2 protein, humanPregnancy ProteinsProto-Oncogene Proteins c-mdm2Ribosomal ProteinsRSL1D1 protein, humanTP53 protein, humanTumor Suppressor Protein p53Cell proliferationCell survivalHDM2mRNA stabilityNucleolar proteinp53Protein-protein interactionProtein-RNA interactionRSL1D1Ubiquitination

Identifiers

PMID34362424
PMCPMC8344204
OpenAlexW3193060693

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.