Evidence map›Paper›PMID 25104022›Full record

ArticleNucleic acids research2014

Arginine methylation of hnRNPK negatively modulates apoptosis upon DNA damage through local regulation of phosphorylation.

Jen-Hao Yang, Yi-Ying Chiou, Shu-Ling Fu, I-Yun Shih, Tsai-Hsuan Weng, Wey-Jinq Lin, Chao-Hsiung Lin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

36 citing papers in PubMed, 54 citations in OpenAlex.

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  11. Structure, Activity, and Function of PRMT1.Life (Basel, Switzerland) · 2021
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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

7 authors at 3 institutions in 1 country.

Jen-Hao YangDepartment of Life Sciences and Institute of Genome Sciences, National Yang Ming University, Taipei 11221, Taiwan.
Yi-Ying ChiouInstitute of Biopharmaceutical Sciences, National Yang Ming University, Taipei 11221, Taiwan.
Shu-Ling FuInstitute of Traditional Medicine, National Yang-Ming University, Taipei 11221, Taiwan.
I-Yun ShihInstitute of Biopharmaceutical Sciences, National Yang Ming University, Taipei 11221, Taiwan.
Tsai-Hsuan WengDepartment of Life Sciences and Institute of Genome Sciences, National Yang Ming University, Taipei 11221, Taiwan.
Wey-Jinq LinInstitute of Biopharmaceutical Sciences, National Yang Ming University, Taipei 11221, Taiwan.
Chao-Hsiung LinDepartment of Life Sciences and Institute of Genome Sciences, National Yang Ming University, Taipei 11221, Taiwan Institute of Biopharmaceutical Sciences, National Yang Ming University, Taipei 11221, Taiwan Proteomics Research Center, National Yang Ming University, Taipei 11221, Taiwan chlin2@ym.edu.tw.
National Yang Ming Chiao Tung University · TWNational Taiwan University · TWNational Yang Ming Chiao Tung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heterogeneous nuclear ribonucleoprotein K (hnRNPK) is an RNA/DNA-binding protein involved in chromatin remodeling, RNA processing and the DNA damage response. In addition, increased hnRNPK expression has been associated with tumor development and progression. A variety of post-translational modifications of hnRNPK have been identified and shown to regulate hnRNPK function, including phosphorylation, ubiquitination, sumoylation and methylation. However, the functional significance of hnRNPK arginine methylation remains unclear. In the present study, we demonstrated that the methylation of two essential arginines, Arg296 and Arg299, on hnRNPK inhibited a nearby Ser302 phosphorylation that was mediated through the pro-apoptotic kinase PKCδ. Notably, the engineered U2OS cells carrying an Arg296/Arg299 methylation-defective hnRNPK mutant exhibited increased apoptosis upon DNA damage. While such elevated apoptosis can be diminished through addition with wild-type hnRNPK, we further demonstrated that this increased apoptosis occurred through both intrinsic and extrinsic pathways and was p53 independent, at least in part. Here, we provide the first evidence that the arginine methylation of hnRNPK negatively regulates cell apoptosis through PKCδ-mediated signaling during DNA damage, which is essential for the anti-apoptotic role of hnRNPK in apoptosis and the evasion of apoptosis in cancer cells.

Indexed as

ApoptosisDNA DamageArginineCaspase 3Cell LineEtoposideHeterogeneous-Nuclear Ribonucleoprotein KHumansMethylationMutationPhosphorylationProtein-Arginine N-MethyltransferasesProtein Kinase C-deltaRepressor ProteinsRibonucleoproteinsArginineCaspase 3EtoposideHeterogeneous-Nuclear Ribonucleoprotein KHNRNPK protein, humanPRMT1 protein, humanProtein-Arginine N-MethyltransferasesProtein Kinase C-deltaRepressor ProteinsRibonucleoproteins

Identifiers

PMID25104022
PMCPMC4150800
OpenAlexW2011878209

What OpenQuestion holds

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LicenceCC BY-NC
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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.