PROTEIN TYROSINE PHOSPHATASES IN CELLULAR SIGNALING

许多细胞表面受体的聚集导致 胞内蛋白质的酪氨酸磷酸化。这个 这些蛋白质的磷酸化状态然后控制酶 活性和蛋白质-蛋白质的缔合或解离 传播和调节下游信号转导。这个 一个分子的蛋白质磷酸化水平是由平衡引起的 蛋白酪氨酸激酶和磷酸酶活性之间的关系。 因此，了解蛋白质的作用很重要。 酪氨酸磷酸酶在信号的启动、维持和调节中的作用 细胞内的转导。在去年的研究中，我们发现 含SH2结构域的蛋白酪氨酸磷酸酶SHP-1 和SHP-2与FceRI关联，并且SHP-2也关联 与黏附分子PECAM-1，即酪氨酸 通过激活不同的整合素或免疫而磷酸化 感受器。

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 FceRI 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.