Evidence map›Paper›PMID 26912789›Full record

ArticleMolecular biology of the cell2016

Cross-talk between Arg methylation and Ser phosphorylation modulates apoptosis signal-regulating kinase 1 activation in endothelial cells.

Ming Chen, Xiaosheng Qu, Zhiqing Zhang, Huayu Wu, Xia Qin, Fuji Li, Zhenfang Liu, Liyuan Tian, Jianhua Miao, Wei Shu

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.1field-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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. SDS3 regulates microglial inflammation by modulating the expression of the upstream kinase ASK1 in the p38 MAPK signaling pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
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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

10 authors at 3 institutions in 1 country.

Ming ChenCenter for Identification of Chinese Herbal Medicines, Guangxi Botanical Garden of Medicinal Plants, Nanning 530023, China Tianjin Institute of Hygiene and Environmental Medicine, Tianjin 300050, China Shuwei7866@126.com mjh1962@vip.163.com chenmingprotein@163.com.
Xiaosheng QuCenter for Identification of Chinese Herbal Medicines, Guangxi Botanical Garden of Medicinal Plants, Nanning 530023, China.
Zhiqing ZhangTianjin Institute of Hygiene and Environmental Medicine, Tianjin 300050, China.
Huayu WuDepartment of Cell Biology and Genetics, Guangxi Medical University, Nanning 530021, China.
Xia QinDepartment of Cell Biology and Genetics, Guangxi Medical University, Nanning 530021, China.
Fuji LiDepartment of Cell Biology and Genetics, Guangxi Medical University, Nanning 530021, China.
Zhenfang LiuDepartment of Hematology, First Affiliated Hospital of Guangxi Medical University, Nanning 530021, China.
Liyuan TianDepartment of Specific Diagnosis, General Hospital of Airforce, Beijing 100142, China.
Jianhua MiaoCenter for Identification of Chinese Herbal Medicines, Guangxi Botanical Garden of Medicinal Plants, Nanning 530023, China Shuwei7866@126.com mjh1962@vip.163.com chenmingprotein@163.com.
Wei ShuDepartment of Cell Biology and Genetics, Guangxi Medical University, Nanning 530021, China Shuwei7866@126.com mjh1962@vip.163.com chenmingprotein@163.com.
Guangxi Medical University · CNGuangxi Medicinal Botanical Garden · CNAir Force General Hospital PLA · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe a novel functional interaction between ASK1 and PRMT5. We show that PRMT5 interacts with and methylates ASK1 at arginine residue 89 and thereby negatively regulates its activity by promoting the interaction between ASK1 and Akt and thus phosphorylating ASK1 at serine residue 83. Furthermore, the association between ASK1 and Akt is enhanced by VEGF stimulation, and PRMT5 is required for this association. Moreover, PRMT5-mediated ASK1 methylation impaired the H2O2-induced activity of ASK1, and this inhibitory effect of PRMT5 was abolished by replacement of arginine 89 with Trp or depletion of PRMT5 expression by RNA interference. Together the results demonstrate cross-talk between arginine methylation and serine phosphorylation in ASK1.

Indexed as

ArginineCell LineEndothelial CellsEnzyme ActivationHumansHydrogen PeroxideMAP Kinase Kinase Kinase 5MethylationPhosphorylationProtein-Arginine N-MethyltransferasesProtein Interaction MappingProto-Oncogene Proteins c-aktSerineSignal TransductionVascular Endothelial Growth Factor AArginineHydrogen PeroxideMAP3K5 protein, humanMAP Kinase Kinase Kinase 5PRMT5 protein, humanProtein-Arginine N-MethyltransferasesProto-Oncogene Proteins c-aktSerineVascular Endothelial Growth Factor A

Identifiers

PMID26912789
PMCPMC4831888
OpenAlexW2289373951

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.