Evidence map›Paper›PMID 26158630›Full record

ArticleNature communications2015

Crucial roles of RSK in cell motility by catalysing serine phosphorylation of EphA2.

Yue Zhou, Naoki Yamada, Tomohiro Tanaka, Takashi Hori, Satoru Yokoyama, Yoshihiro Hayakawa, Seiji Yano, Junya Fukuoka, Keiichi Koizumi, Ikuo Saiki and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 147 citations in OpenAlex.

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  15. Development of an anti-human EphA2 monoclonal antibody EaBiochemistry and biophysics reports · 2025
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27 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Yue ZhouDepartment of Cancer Cell Biology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Japan.
Naoki YamadaDepartment of Cancer Cell Biology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Japan.
Tomohiro TanakaDepartment of Cancer Cell Biology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Japan.
Takashi HoriDepartment of Diagnostic Pathology, Toyama University Hospital, Toyama 930-0194, Japan.
Satoru YokoyamaDivision of Pathogenic Biochemistry, Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan.
Yoshihiro HayakawaDivision of Pathogenic Biochemistry, Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan.
Seiji YanoDivision of Medical Oncology, Cancer Research Institute, Kanazawa University, Kanazawa 920-8641, Japan.
Junya FukuokaDepartment of Pathology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8501, Japan.
Keiichi KoizumiDivision of Kampo Diagnostics, Institute of Natural Medicine, University of Toyama 930-0194, Toyama, Japan.
Ikuo SaikiDivision of Pathogenic Biochemistry, Institute of Natural Medicine, University of Toyama, Toyama 930-0194, Japan.
Hiroaki SakuraiDepartment of Cancer Cell Biology, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Japan.
University of Toyama · JPNagasaki University · JPToyama University Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crosstalk between inflammatory signalling pathways and receptor tyrosine kinases has been revealed as an indicator of cancer malignant progression. In the present study, we focus on EphA2 receptor tyrosine kinase, which is overexpressed in many human cancers. It has been reported that ligand-independent phosphorylation of EphA2 at Ser-897 is induced by Akt. We show that inflammatory cytokines promote RSK-, not Akt-, dependent phosphorylation of EphA2 at Ser-897. In addition, the RSK-EphA2 signalling pathway controls cell migration and invasion of metastatic breast cancer cells. Moreover, Ser-897-phosphorylated EphA2 co-localizes with phosphorylated active form of RSK in various human tumour specimens, and this double positivity is related to poor survival in lung cancer patients, especially those with a smoking history. Taken together, these results indicate that the phosphorylation of EphA2 at Ser-897 is controlled by RSK and the RSK-EphA2 axis might contribute to cell motility and promote tumour malignant progression.

Indexed as

Breast NeoplasmsCarcinoma, Non-Small-Cell LungCatalysisCell Line, TumorCell MovementCytokinesFemaleHEK293 CellsHeLa CellsHumansInflammation MediatorsLiver NeoplasmsLung NeoplasmsMaleNeoplasmsPhosphorylationCytokinesInflammation MediatorsReceptor, EphA2ribosomal protein S6 kinase, 90kDa, polypeptide 3Ribosomal Protein S6 Kinases, 90-kDaRPS6KA1 protein, humanSerine

Identifiers

PMID26158630
PMCPMC4510653
OpenAlexW1088509254

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.