Evidence map›Paper›PMID 31125786›Full record

ArticleNeoplasia (New York, N.Y.)2019

SUMOylation of Csk Negatively Modulates its Tumor Suppressor Function.

Nan Cui, Tianqi Liu, Yanmin Guo, Jinzhuo Dou, Qianqian Yang, Hailong Zhang, Ran Chen, Yanli Wang, Xian Zhao, Jianxiu Yu and 1 more

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Regulation, targets and functions of CSK.Frontiers in cell and developmental biology · 2023
    Review
  3. CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023
    Review
  4. Apoptosis regulation by the tyrosine-protein kinase CSK.Frontiers in cell and developmental biology · 2022
    Review
  5. Article
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 1 institution in 1 country.

Nan CuiDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Tianqi LiuDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Yanmin GuoDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Jinzhuo DouDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Qianqian YangDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Hailong ZhangDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Ran ChenDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Yanli WangDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Xian ZhaoDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China.
Jianxiu YuDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China. Electronic address: Jianxiu.Yu@gmail.com.
Jian HuangDepartment of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory of Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine (SJTU-, SM), Shanghai, 200025, China. Electronic address: jyhuanj@shsmu.edu.cn.
Shanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Csk, a non-receptor tyrosine kinase, serves as an indispensable negative regulator of the Src family kinases (SFKs). However, little is known about regulation of Csk expression so far. SUMOylation, a reversible post-translational modification, has been shown to regulate many biological processes especially in tumor progression. Here we report that Csk is covalently modified by SUMO1 at lysine 53 (K53) both in vitro and in vivo. Treatment with hydrogen peroxide inhibited this modification to a certain extent, but PIAS3, identified as the main specific SUMO E3 ligase for Csk, could significantly enhance SUMO1-Csk level. In addition, phosphorylation at Ser364, the active site in Csk, had no effect on this modification. Ectopic expression of SUMO-defective mutant, Csk

Indexed as

CSK Tyrosine-Protein KinaseHumansHydrogen PeroxideLysineMolecular ChaperonesNeoplasmsPhosphorylationProtein BindingProtein Inhibitors of Activated STATProtein Processing, Post-TranslationalSmall Ubiquitin-Related Modifier Proteinssrc-Family KinasesSUMO-1 ProteinSumoylationUbiquitin-Protein LigasesCSK protein, humanCSK Tyrosine-Protein KinaseHydrogen PeroxideLysineMolecular ChaperonesPIAS1 protein, humanProtein Inhibitors of Activated STATSmall Ubiquitin-Related Modifier Proteinssrc-Family KinasesSUMO-1 ProteinSUMO1 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID31125786
PMCPMC6531875
OpenAlexW2945751782

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.