Evidence map›Paper›PMID 35073964›Full record

ArticleJournal of experimental & clinical cancer research : CR2022

Loss of RPS27a expression regulates the cell cycle, apoptosis, and proliferation via the RPL11-MDM2-p53 pathway in lung adenocarcinoma cells.

Hongyan Li, Hong Zhang, Guomin Huang, Zhitong Bing, Duling Xu, Jiadi Liu, Hongtao Luo, Xiaoli An

Open access · goldAbstract read
In one paragraph

Article in Journal of experimental & clinical cancer research : CR, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 83 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

8 authors at 2 institutions in 1 country.

Hongyan LiDepartment of Medical Physics, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China.
Hong ZhangDepartment of Medical Physics, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China. zhangh@impcas.ac.cn.
Guomin HuangDepartment of Medical Physics, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China.
Zhitong BingSchool of Nuclear Science and Technology, University of Chinese Academy of Sciences, Beijing, 101408, China.
Duling XuDepartment of Medical Physics, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China.
Jiadi LiuDepartment of Medical Physics, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China.
Hongtao LuoDepartment of Radiation Medicine, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China.
Xiaoli AnDepartment of Computational Physics, Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou, 730000, China.
Chinese Academy of Sciences · CNInstitute of Modern Physics · CN

Funding

the key program of the national natural science foundation of china U1632270the National Key R&D Program of China 2018YFE0205100the national laboratory of heavy ion accelerator of lanzhou E0HIRFL03Pthe national natural science foundation of china 11505244the national natural science foundation of china 11875061the national natural science foundation of gansu province 20JR5RA550
6 · The paper itself

Abstract

backgroundDepletion of certain ribosomal proteins induces p53 activation, which is mediated mainly by ribosomal protein L5 (RPL5) and/or ribosomal protein L11 (RPL11). Therefore, RPL5 and RPL11 may link RPs and p53 activation. Thus, this study aimed to explore whether RPs interact with RPL11 and regulate p53 activation in lung adenocarcinoma (LUAD) cells.

methodsThe endogenous RPL11-binding proteins in A549 cells were pulled down through immunoprecipitation and identified with a proteomics approach. Docking analysis and GST-fusion protein assays were used to analyze the interaction of ribosomal protein S27a (RPS27a) and RPL11. Co-immunoprecipitation and in vitro ubiquitination assays were used to detect the effects of knockdown of RPS27a on the interaction between RPS27a and RPL11, and on p53 accumulation. Cell cycle, apoptosis, cell invasion and migration, cell viability and colony-formation assays were performed in the presence of knockdown of RPS27a. The RPS27a mRNA expression in LUAD was analyzed on the basis of the TCGA dataset, and RPS27a expression was detected through immunohistochemistry in LUAD samples. Finally, RPS27a and p53 expression was analyzed through immunohistochemistry in A549 cell xenografts with knockdown of RPS27a.

resultsRPS27a was identified as a novel RPL11 binding protein. GST pull-down assays revealed that RPS27a directly bound RPL11. Knockdown of RPS27a weakened the interaction between RPS27a and RPL11, but enhanced the binding of RPL11 and murine double minute 2 (MDM2), thereby inhibiting the ubiquitination and degradation of p53 by MDM2. Knockdown of RPS27a stabilized p53 in an RPL11-dependent manner and induced cell viability inhibition, cell cycle arrest and apoptosis in a p53-dependent manner in A549 cells. The expression of RPS27a was upregulated in LUAD and correlated with LUAD progression and poorer prognosis. Overexpression of RPS27a correlated with upregulation of p53, MDM2 and RPL11 in LUAD clinical specimens. Knockdown of RPS27a increased p53 activation, thus, suppressing the formation of A549 cell xenografts in nude mice.

conclusionsRPS27a interacts with RPL11, and RPS27a knockdown enhanced the binding of RPL11 and MDM2, thereby inhibiting MDM2-mediated p53 ubiquitination and degradation; in addition, RPS27a as important roles in LUAD progression and prognosis, and may be a therapeutic target for patients with LUAD.

Indexed as

Adenocarcinoma of LungAnimalsApoptosisCell CycleCell ProliferationFemaleHumansLung NeoplasmsMiceMice, NudeRibosomal ProteinsSurvival AnalysisTransfectionribosomal protein L11Ribosomal Proteinsribosomal protein S27aApoptosisLung adenocarcinomaRibosomal protein S27a (RPS27a)

Identifiers

PMID35073964
PMCPMC8785590
OpenAlexW4207042123

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.