Schnepp B, Donaldson T, Grumbling G, Ostrowski S, Schweitzer R, Shilo B Z, Simcox A
Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210 USA.
Genes Dev. 1998 Apr 1;12(7):908-13. doi: 10.1101/gad.12.7.908.
In Drosophila the function of the epidermal growth factor (EGF) receptor is modulated zygotically by three EGF-like proteins: Spitz (Spi), which is a potent activator; Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. Chimeric molecules were constructed in which the EGF domain of Vn was swapped with the EGF domain from each factor. The modified Vn proteins behaved both in vitro and in vivo with properties characteristic of the factor from which the EGF domain was derived. These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties.
在果蝇中，表皮生长因子（EGF）受体的功能由三种类表皮生长因子蛋白合子调控：强效激活剂斯皮茨（Spi）；中度激活剂静脉（Vn）；抑制剂阿戈斯（Aos）。构建了嵌合分子，其中Vn的EGF结构域与每个因子的EGF结构域进行了交换。修饰后的Vn蛋白在体外和体内均表现出源自其EGF结构域的因子所特有的特性。这些结果表明，EGF结构域是赋予DER抑制剂和激活剂独特特性的关键决定因素。
