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首页> 外文期刊>Molecular and Cellular Biology >Shc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells.
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Shc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells.

机译：Shc，Grb2，Sos1和150公斤的酪氨酸磷酸化蛋白与Fms在造血细胞中形成复合物。

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Fms, the macrophage colony-stimulating factor (M-CSF) receptor, is normally expressed in myeloid cells and initiates signals for both growth and development along the monocyte/macrophage lineage. We have examined Fms signal transduction pathways in the murine myeloid progenitor cell line FDC-P1. M-CSF stimulation of FDC-P1 cells expressing exogenous Fms resulted in tyrosine phosphorylation of a variety of cellular proteins in addition to Fms. M-CSF stimulation also resulted in Fms association with two of these tyrosine-phosphorylated proteins, one of which was identified as the 55-kDa Shc, which is shown in other systems to be involved in growth stimulation, and the other was a previously uncharacterized 150-kDa protein (p150). Fms also formed complexes with Grb2 and Sos1, and neither contained phosphotyrosine. Whereas both Grb2 and Sos1 complexed with Fms only after M-CSF stimulation, the amount of Sos1 complexed with Grb2 was not M-CSF dependent. Shc coimmunoprecipitated Sos1, Grb2, and tyrosine-phosphorylated p150, while Grb2 immunoprecipitates contained mainly phosphorylated p150, Fms, Shc, and Sos1. Shc interacted with tyrosine-phosphorylated p150 via its SH2 domain, and the Grb2 SH2 domain likewise bound tyrosine-phosphorylated Fms and p150. Analysis of Fms mutated at each of four tyrosine autophosphorylation sites indicated that none of these sites dramatically affected p150 phosphorylation or its association with Shc and Grb2. M-CSF stimulation of fibroblast cell lines expressing exogenous murine Fms did not phosphorylate p150, and this protein was not detected either in cell lysates or in Grb2 or Shc immunoprecipitates. The p150 protein is not related to known signal transduction molecules and may be myeloid cell specific. These results suggest that M-CSF stimulation of myeloid cells could activate Ras through the nucleotide exchange factor Sos1 by Grb2 binding to either Fms, Shc, or p150 and that Fms signal transduction in myeloid cells differs from that in fibroblasts.
机译：Fms是巨噬细胞集落刺激因子（M-CSF）受体，通常在髓样细胞中表达，并引发沿单核/巨噬细胞谱系生长和发育的信号。我们已经检查了小鼠骨髓祖细胞FDC-P1中的Fms信号转导途径。 M-CSF刺激表达外源性Fms的FDC-P1细胞导致除Fms之外的多种细胞蛋白的酪氨酸磷酸化。 M-CSF刺激还导致Fms与这些酪氨酸磷酸化蛋白中的两种相关，其中一种被鉴定为55-kDa Shc，在其他系统中显示与生长刺激有关，而另一种以前未鉴定150 kDa蛋白（p150）。 Fms还与Grb2和Sos1形成复合物，并且都不包含磷酸酪氨酸。仅在M-CSF刺激后，Grb2和Sos1才与Fms形成复合物，而与Grb2结合的Sos1的量则不受M-CSF依赖性。 Shc共沉淀Sos1，Grb2和酪氨酸磷酸化的p150，而Grb2免疫沉淀主要含有p150，Fms，Shc和Sos1磷酸化。 Shc通过其SH2结构域与酪氨酸磷酸化的p150相互作用，而Grb2 SH2结构域同样结合酪氨酸磷酸化的Fms和p150。对在四个酪氨酸自磷酸化位点的每一个突变的Fms的分析表明，这些位点均未显着影响p150磷酸化或其与Shc和Grb2的缔合。表达外源鼠Fms的成纤维细胞系的M-CSF刺激不会使p150磷酸化，并且在细胞裂解液或Grb2或Shc免疫沉淀物中均未检测到该蛋白。 p150蛋白与已知的信号转导分子无关，可能是髓样细胞特异性的。这些结果表明，骨髓细胞的M-CSF刺激可以通过与Fms，Shc或p150结合的Grb2通过核苷酸交换因子Sos1激活Ras，并且骨髓细胞中Fms信号转导与成纤维细胞不同。

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