高尔基蛋白 FAPP2 管状化膜。
Golgi protein FAPP2 tubulates membranes.
机构信息
Max Planck Institute for Molecular Cell Biology and Genetics, Dresden, Germany.
出版信息
Proc Natl Acad Sci U S A. 2009 Dec 15;106(50):21121-5. doi: 10.1073/pnas.0911789106. Epub 2009 Nov 25.
Abstract
The Golgi-associated four-phosphate adaptor protein 2 (FAPP2) has been shown to possess transfer activity for glucosylceramide both in vitro and in cells. We have previously shown that FAPP2 is involved in apical transport from the Golgi complex in epithelial MDCK cells. In this paper we assign an unknown activity for the protein as well as providing structural insight into protein assembly and a low-resolution envelope structure. By applying analytical ultracentrifugation and small-angle x-ray scattering, we show that FAPP2 is a dimeric protein in solution, having a curved shape 30 nm in length. The purified FAPP2 protein has the capability to form tubules from membrane sheets in vitro. This activity is dependent on the phosphoinositide-binding activity of the PH domain of FAPP2. These data suggest that FAPP2 functions directly in the formation of apical carriers in the trans-Golgi network.
摘要
高尔基相关四磷酸接头蛋白 2（FAPP2）已被证明在体外和细胞内具有葡萄糖神经酰胺的转移活性。我们之前已经表明，FAPP2 参与了上皮细胞系 MDCK 细胞中从高尔基复合体到顶侧的运输。在本文中，我们将该蛋白的未知活性进行了分配，并提供了蛋白质组装和低分辨率包膜结构的结构见解。通过应用分析超速离心和小角度 X 射线散射，我们表明 FAPP2 在溶液中是二聚体蛋白，其形状为 30nm 长的弯曲形状。纯化的 FAPP2 蛋白具有在体外从膜片中形成小管的能力。该活性依赖于 FAPP2 PH 结构域与磷酸肌醇结合的活性。这些数据表明 FAPP2 直接参与了形成反式高尔基体网络中的顶侧载体。
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