Signal Transduction In Mast Cells

肥大细胞通过释放一系列介质在许多炎症和免疫反应中发挥重要作用。我们研究的目的是了解导致这些分子释放的细胞内信号转导途径。在之前的研究中，我们观察到蛋白酪氨酸磷酸化是FceRI诱导脱颗粒的早期和关键信号。酪氨酸蛋白激酶Syk在受体聚集后被酪氨酸磷酸化并被激活。Syk也被证明是受体诱导的炎症介质释放所必需的。最近的研究表明，接头蛋白Gab2被发现与几种信号分子相关，包括蛋白酪氨酸激酶和磷酸酶。这种相互作用被证明是Gab2作为细胞信号通路调节器的重要功能。研究还定义了信号分子下调的机制，这是由于一种称为泛素化的过程而发生的，在泛素化过程中，分子被共价偶联蛋白标记，以降解为目标。

Mast cells play an important role in many inflammatory and immunological reactions by releasing an array of mediators. The goal of our studies is to understand the intracellular signal transduction pathways that lead to the release of these molecules. In previous studies we observed that protein tyrosine phosphorylation is an early and critical signal for FceRI induced degranulation. The protein tyrosine kinase Syk was found to be tyrosine phosphorylated and activated after receptor aggregation. Syk was also shown to be essential for the receptor-induced release of inflammatory mediators. Recent studies demonstrated that the adaptor protein Gab2 was found to associate with several signaling molecules including protein tyrosine kinases and phosphatases. Such interactions were shown to be important for Gab2 to function as a regulator of signaling pathways in cells. Studies also defined the mechanisms for the down regulation of signaling molecules that occurs due to a process called ubiquitination whereby molecules are tagged by a covalently coupled protein that targets them for degradation.