Cell Biology, Division of Life Science, Graduate School of Natural Science and Technologies, Kanazawa University, Japan.
J Pharmacol Sci. 2010;112(3):255-64. doi: 10.1254/jphs.09r03cr. Epub 2010 Mar 2.
GM130 is a peripheral membrane protein strongly attached to the Golgi membrane and is isolated from the detergent and salt resistant Golgi matrix. GM130 is rich in coiled-coil structures and predicted to take a rod-like shape. Together with p115, giantin, and GRASP65, GM130 facilitates vesicle fusion to the Golgi membrane as a vesicle "tethering factor". GM130 is also involved in the maintenance of the Golgi structure and plays a major role in the disassembly and reassembly of the Golgi apparatus during mitosis. Emerging evidence suggests that GM130 is involved in the control of glycosylation, cell cycle progression, and higher order cell functions such as cell polarization and directed cell migration. This creates the potential for novel Golgi-targeted drugs and treatments for various diseases including glycosylation defects, immune diseases, and cancer.
GM130 是一种外周膜蛋白，与高尔基体膜紧密结合，可从去污剂和耐盐的高尔基体基质中分离出来。GM130 富含卷曲螺旋结构，预测呈杆状。GM130 与 p115、巨大蛋白和 GRASP65 一起，作为囊泡“连接因子”促进囊泡与高尔基体膜融合。GM130 还参与高尔基体结构的维持，并在有丝分裂过程中高尔基体装置的拆卸和重新组装中起主要作用。新出现的证据表明，GM130 参与糖基化的控制、细胞周期进程以及更高阶的细胞功能，如细胞极化和定向细胞迁移。这为各种疾病（包括糖基化缺陷、免疫疾病和癌症）的新型靶向高尔基体的药物和治疗方法创造了潜力。
