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

• Ikeda, Osamu

• Sekine, Yuichi

• Kakisaka, Michinori

• Tsuji, Satoshi

• Muromoto, Ryuta

• Ohbayashi, Norihiko

• Oritani, Kenji

• Yoshimura, Akihiko

• Matsuda, Tadashi

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.

Journal

• Biochemical and Biophysical Research Communications

  Biochemical and Biophysical Research Communications 358 (3), 931-937, 2007-07-06

  Elsevier Inc.

Keywords

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

Details

• CRID: 1050845763915974656
• NII Article ID: 120000969065
• ISSN: 10902104
• ISSN: 0006291X
• HANDLE: 2115/22099
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles