Evidence map›Paper›PMID 32994405›Full record

ArticleSignal transduction and targeted therapy2020

The cross-talk between methylation and phosphorylation in lymphoid-specific helicase drives cancer stem-like properties.

Na Liu, Rui Yang, Ying Shi, Ling Chen, Yating Liu, Zuli Wang, Shouping Liu, Lianlian Ouyang, Haiyan Wang, Weiwei Lai and 9 more

Open access · goldAbstract read
In one paragraph

Article in Signal transduction and targeted therapy, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

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  18. FAIMS Enhances the Detection of PTM Crosstalk Sites.Journal of proteome research · 2022
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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

19 authors at 3 institutions in 1 country.

Na LiuDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Rui YangDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Ying ShiDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Ling ChenDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Yating LiuDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Zuli WangDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Shouping LiuDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Lianlian OuyangDepartment of Oncology, Institute of Medical Sciences, National Clinical Research Center for Geriatric Disorders, Xiangya Hospital, Central South University, 410008, Changsha, Hunan, China.
Haiyan WangDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Weiwei LaiDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Chao MaoDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Min WangDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Yan ChengXiangya School of Pharmaceutical Sciences, Central South University, 410078, Changsha, China.
Shuang LiuDepartment of Oncology, Institute of Medical Sciences, National Clinical Research Center for Geriatric Disorders, Xiangya Hospital, Central South University, 410008, Changsha, Hunan, China.
Xiang WangHunan Key Laboratory of Tumor Models and Individualized Medicine; Hunan Key Laboratory of Early Diagnosis and Precision Therapy in Lung Cancer, Department of Thoracic Surgery, Second Xiangya Hospital, Central South University, 410011, Changsha, China.
Hu ZhouShanghai Institute of Material Medical, Chinese Academy of Sciences (CAS), 555 Zuchongzhi Road, Zhangjiang Hi-Tech Park, 201203, Shanghai, China.
Ya CaoDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China.
Desheng XiaoDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China. xdsh96@21cn.com.
Yongguang TaoDepartment of Pathology, Key Laboratory of Carcinogenesis and Cancer Invasion (Ministry of Education), Xiangya Hospital; Central South University, 410078, Hunan, China. taoyong@csu.edu.cn.
Central South University · CNXiangya Hospital Central South University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational modifications (PTMs) of proteins, including chromatin modifiers, play crucial roles in the dynamic alteration of various protein properties and functions including stem-cell properties. However, the roles of Lymphoid-specific helicase (LSH), a DNA methylation modifier, in modulating stem-like properties in cancer are still not clearly clarified. Therefore, exploring PTMs modulation of LSH activity will be of great significance to further understand the function and activity of LSH. Here, we demonstrate that LSH is capable to undergo PTMs, including methylation and phosphorylation. The arginine methyltransferase PRMT5 can methylate LSH at R309 residue, meanwhile, LSH could as well be phosphorylated by MAPK1 kinase at S503 residue. We further show that the accumulation of phosphorylation of LSH at S503 site exhibits downregulation of LSH methylation at R309 residue, which eventually promoting stem-like properties in lung cancer. Whereas, phosphorylation-deficient LSH S503A mutant promotes the accumulation of LSH methylation at R309 residue and attenuates stem-like properties, indicating the critical roles of LSH PTMs in modulating stem-like properties. Thus, our study highlights the importance of the crosstalk between LSH PTMs in determining its activity and function in lung cancer stem-cell maintenance.

Indexed as

AnimalsCell Line, TumorDNA HelicasesFemaleHumansLung NeoplasmsMethylationMiceMice, NudeNeoplasm ProteinsNeoplastic Stem CellsPhosphorylationDNA HelicasesHELLS protein, humanNeoplasm Proteins

Identifiers

PMID32994405
PMCPMC7524730
OpenAlexW3090908606

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.