Kyushu University · 의학
요시노리 후쿠이 교수의 연구실은 신호전달 분자인 DOCK2와 라크 단백질을 중심으로 세포 이동성과 면역 반응의 분자 기전을 규명하고 있습니다. 특히, DOCK2가 세균 유도성 세포 이동과 항바이러스 면역 반응에서 핵심적으로 작용하는 메커니즘을 밝혀내며, 인지질 대사와의 상호작용을 통해 세포 골격 재편성과 신호 전파를 조절하는 원리를 연구하고 있습니다. 또한, 온코진 단백질인 p60v-src와 관련된 인지질 키나제 활성 및 세분화된 단백질 상호작용 메커니즘을 통해 세포의 악성 전환과 신호 전달 네트워크의 기초를 다지고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
During chemotaxis, activation of the small guanosine triphosphatase Rac is spatially regulated to organize the extension of membrane protrusions in the direction of migration. In neutrophils, Rac activation is primarily mediated by DOCK2, an atypical guanine nucleotide exchange factor. Upon stimulation, we found that DOCK2 rapidly translocated to the plasma membrane in a phosphatidylinositol 3,4,5-trisphosphate-dependent manner. However, subsequent accumulation of DOCK2 at the leading edge requi
Immunoprecipitates of p60v-src proteins from chicken embryo fibroblasts infected with Rous sarcoma virus were assayed for phosphatidylinositol (PI) kinase activity in the absence of detergents. The product of the PI kinase reaction, phosphatidylinositol monophosphate (PIP), migrated slightly slower than did the authentic phosphatidylinositol-4-monophosphate marker in thin-layer chromatography and was indistinguishable from phosphatidylinositol-3-monophosphate produced by PI kinase type I. Furthe
Plasmacytoid dendritic cells (pDCs) play a key role in antiviral immunity, but also contribute to the pathogenesis of certain autoimmune diseases, by producing large amounts of type I IFNs. Although activation of pDCs is triggered by engagement of nucleotide-sensing toll-like receptors (TLR) 7 and 9, type I IFN induction additionally requires IkappaB kinase (IKK) alpha-dependent activation of IFN regulatory factor (IRF) 7. However, the signaling pathway mediating IKK-alpha activation is poorly d
We have assayed immunoprecipitates of several oncogene products from retrovirally infected chicken embryo fibroblasts (CEF) for phosphatidylinositol (PI) kinase activity. Immunoprecipitates of P68gag-ros, P130gag-tps, P47gag-crk, polyoma middle T (mT)-p60c-src complex, and mT-p62c-yrs complex exhibited PI kinase activity when assayed without detergents. This activity was sensitive to the nonionic detergent, Triton X-100, and the product was indistinguishable from phosphatidylinositol-3-phosphate
When purified p60v-src was mixed with lysates of chicken embryo fibroblasts and immunoprecipitated with anti-Src antibody, phosphatidylinositol (PI)-3 kinase activity was found to be present in the Src protein immunoprecipitates. The level of bound PI-3 kinase activity was 5 to 10 times higher in lysates obtained from cells transformed by the src, fps, or yes oncogene than in lysates of uninfected cells. This increase in associated PI-3 kinase activity appears to be due to increased binding of t
p60v-src has been shown to associate with a detergent-insoluble cellular matrix containing cytoskeletal proteins, but p60c-src does not bind to this matrix. We analyzed the association of mutant src proteins with the matrix and found that mutants which lack an amino-terminal portion (residues 149 to 169) of the SH2 domain cannot bind to the matrix. Neither the SH3 region nor other portions of the SH2 region were required for association. We also tested protein kinase-defective mutants and chimer
