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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Stimulation of human monocytes with macrophage colony-stimulating factor induces a Grb2-mediated association of the focal adhesion kinase pp125FAK and dynamin.
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Stimulation of human monocytes with macrophage colony-stimulating factor induces a Grb2-mediated association of the focal adhesion kinase pp125FAK and dynamin.

机译：用巨噬细胞集落刺激因子刺激人单核细胞诱导了Grb2介导的粘着斑激酶pp125FAK和动力蛋白的缔合。

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摘要

Macrophage colony-stimulating factor (M-CSF) is required for the growth and differentiation of mononuclear phagocytes. In the present studies using human monocytes, we show that M-CSF induces interaction of the Grb2 adaptor protein with the focal adhesion kinase pp125FAK. The results demonstrate that tyrosine-phosphorylated pp125FAK directly interacts with the SH2 domain of Grb2. The findings indicate that a pYENV site at Tyr-925 in pp125FAK is responsible for this interaction. We also demonstrate that the Grb2-FAK complex associates with the GTPase dynamin. Dynamin interacts with the SH3 domains of Grb2 and exhibits M-CSF-dependent tyrosine phosphorylation in association with pp125FAK. These findings suggest that M-CSF-induced signaling involves independent Grb2-mediated pathways, one leading to Ras activation and another involving pp125FAK and a GTPase implicated in receptor internalization.
机译：巨噬细胞集落刺激因子（M-CSF）是单核吞噬细胞生长和分化所必需的。在当前使用人类单核细胞的研究中，我们显示M-CSF诱导Grb2衔接蛋白与粘着斑激酶pp125FAK相互作用。结果表明酪氨酸磷酸化的pp125FAK直接与Grb2的SH2域相互作用。研究结果表明，pp125FAK中Tyr-925的pYENV位点负责这种相互作用。我们还证明了Grb2-FAK复合物与GTPase动力相关。动力蛋白与Grb2的SH3结构域相互作用，并与pp125FAK结合，表现出M-CSF依赖性酪氨酸磷酸化。这些发现表明，M-CSF诱导的信号传导涉及独立的Grb2介导的途径，一个导致Ras激活，另一个涉及pp125FAK和GTPase参与受体内在化。

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