PROTEIN TYROSINE PHOSPHATASES IN CELLULAR SIGNALING

许多细胞表面受体的聚集导致酪氨酸 细胞内蛋白质的磷酸化。蛋白的磷酸化状态 这些蛋白质然后控制酶的活性和蛋白质-蛋白质。 联合或解离，从而向下游传播和调节 信号转导。分子的蛋白质磷酸化水平 是由于蛋白酪氨酸激酶和磷酸酶之间的平衡 活动。因此，重要的是要了解 蛋白酪氨酸磷酸酶在启动、维持和调节中的作用 细胞内的信号转导。在去年的研究中，我们发现 含有SH2结构域的蛋白酪氨酸磷酸酶SHP-1和SHP-1- 2与FC-epsilon-RI关联，并且SHP-2还与 活化酪氨酸磷酸化的黏附分子PECAM-1 不同的整合素或免疫受体。

Aggregation of many cell surface receptors results in tyrosine phosphorylation of intracellular proteins. The phosphorylation state of these proteins then controls enzymatic activity and protein-protein association or dissociation thereby propagating and regulating downstream signal transduction. The level of protein phosphorylation of a molecule is due to the balance between protein tyrosine kinase and phosphatase activities. Therefore, it is important to understand the role of the protein tyrosine phosphatases in initiating, maintaining and regulating signal transduction in cells. In studies during this last year we found that the SH2 domain containing protein tyrosine phosphatase SHP-1 and SHP- 2 associate with Fc-epsilon-RI and that the SHP-2 also associates with the adhesion molecule PECAM-1 that is tyrosine phosphorylated by activation of different integrin or immune receptors.