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

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Title: STAP-2 regulates c-Fms/M-CSF receptor signaling in murine macrophage Raw 264.7 cells.
Authors: Ikeda, Osamu Browse this author
Sekine, Yuichi Browse this author
Kakisaka, Michinori Browse this author
Tsuji, Satoshi Browse this author
Muromoto, Ryuta Browse this author
Ohbayashi, Norihiko Browse this author
Oritani, Kenji Browse this author
Yoshimura, Akihiko Browse this author
Matsuda, Tadashi Browse this author →KAKEN DB
Keywords: Macrophage
Tyrosine phosphorylation
Adaptor protein
Signal transduction
Issue Date: 6-Jul-2007
Publisher: Elsevier Inc.
Journal Title: Biochemical and Biophysical Research Communications
Volume: 358
Issue: 3
Start Page: 931
End Page: 937
Publisher DOI: 10.1016/j.bbrc.2007.05.030
PMID: 17512498
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.
Type: article (author version)
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 松田 正

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