STAP-2 regulates c-Fms/M-CSF receptor signaling in murine macrophage Raw 264.7 cells

Osamu Ikeda, Yuichi Sekine, Michinori Kakisaka, Satoshi Tsuji, Ryuta Muromoto, Norihiko Ohbayashi, Kenji Oritani, Akihiko Yoshimura, Tadashi Matsuda

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    Signal-transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein as a c-Fms/M-CSF receptor-interacting protein and constitutively expressed in macrophages. Our previous studies also revealed that STAP-2 binds to MyD88 and IKK-α/β, and modulates NF-κB signaling in macrophages. In the present study, we examined physiological roles of the interaction between STAP-2 and c-Fms in Raw 264.7 macrophage cells. Our immunoprecipitation has revealed that c-Fms directly interacts with the PH domain of STAP-2 independently on M-CSF-stimulation. Ectopic expression of STAP-2 markedly suppressed M-CSF-induced tyrosine phosphorylation of c-Fms as well as activation of Akt and extracellular signal regulated kinase. In addition, Raw 264.7 cells over-expressing STAP-2 showed impaired migration in response to M-CSF and wound-healing process. Taken together, our findings demonstrate that STAP-2 directly binds to c-Fms and interferes with the PI3K signaling, which leads to macrophage motility, in Raw 264.7 cells.

    Original languageEnglish
    Pages (from-to)931-937
    Number of pages7
    JournalBiochemical and biophysical research communications
    Volume358
    Issue number3
    DOIs
    Publication statusPublished - 2007 Jul 6

    Keywords

    • Adaptor protein
    • Macrophage
    • Migration
    • Signal transduction
    • Tyrosine phosphorylation
    • c-Fms

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Fingerprint Dive into the research topics of 'STAP-2 regulates c-Fms/M-CSF receptor signaling in murine macrophage Raw 264.7 cells'. Together they form a unique fingerprint.

    Cite this