SYK autophosphorylates

Binding of Syk causes conformational changes that lead to Syk activation by autophosphorylation. Syk can be activated by a number of phosphorylation events, and it has been proposed that Syk may function as a switch whereby any of several possible stimuli trigger the acquisition of similar activated conformations. (Tsang et al. 2008). These phosphorylations both modulate Syk's catalytic activity (Keshvara et al. 1997) and generate docking sites for SH2 domain-containing proteins, such as c-Cbl, PLC, and Vav1.

Syk tyrosine phosphorylation is reduced in the presence of the ITIM-containing immunoglobulin superfamily transmembrane protein G6B (Mori et al. 2008).

Syk的结合引发构象变化，进而通过自磷酸化激活Syk。Syk可通过多种磷酸化事件被激活，有研究表明Syk可能作为一种开关，由多种可能的刺激触发其获得类似的激活构象。（Tsang et al. 2008）。这些磷酸化作用不仅调节Syk的催化活性（Keshvara et al. 1997），而且为包含SH2结构域的蛋白质，如c-Cbl、PLC和Vav1，提供了结合位点。Syk的酪氨酸磷酸化在存在ITIM结构域的免疫球蛋白超家族跨膜蛋白G6B时减少（Mori et al. 2008）。