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

Author

Listed:
  • Yue Zhou

    (Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama)

  • Naoki Yamada

    (Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama)

  • Tomohiro Tanaka

    (Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama)

  • Takashi Hori

    (Toyama University Hospital)

  • Satoru Yokoyama

    (Institute of Natural Medicine, University of Toyama)

  • Yoshihiro Hayakawa

    (Institute of Natural Medicine, University of Toyama)

  • Seiji Yano

    (Cancer Research Institute, Kanazawa University)

  • Junya Fukuoka

    (Nagasaki University Graduate School of Biomedical Sciences)

  • Keiichi Koizumi

    (Institute of Natural Medicine, University of Toyama)

  • Ikuo Saiki

    (Institute of Natural Medicine, University of Toyama)

  • Hiroaki Sakurai

    (Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama)

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.

Suggested Citation

  • Yue Zhou & Naoki Yamada & Tomohiro Tanaka & Takashi Hori & Satoru Yokoyama & Yoshihiro Hayakawa & Seiji Yano & Junya Fukuoka & Keiichi Koizumi & Ikuo Saiki & Hiroaki Sakurai, 2015. "Crucial roles of RSK in cell motility by catalysing serine phosphorylation of EphA2," Nature Communications, Nature, vol. 6(1), pages 1-12, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8679
    DOI: 10.1038/ncomms8679
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    Cited by:

    1. Sergi Marco & Matthew Neilson & Madeleine Moore & Arantxa Perez-Garcia & Holly Hall & Louise Mitchell & Sergio Lilla & Giovani R. Blanco & Ann Hedley & Sara Zanivan & Jim C. Norman, 2021. "Nuclear-capture of endosomes depletes nuclear G-actin to promote SRF/MRTF activation and cancer cell invasion," Nature Communications, Nature, vol. 12(1), pages 1-19, December.
    2. Bernhard C. Lechtenberg & Marina P. Gehring & Taylor P. Light & Christopher R. Horne & Mike W. Matsumoto & Kalina Hristova & Elena B. Pasquale, 2021. "Regulation of the EphA2 receptor intracellular region by phosphomimetic negative charges in the kinase-SAM linker," Nature Communications, Nature, vol. 12(1), pages 1-16, December.

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