Golgi protein FAPP2 tubulates membranes
Golgi protein FAPP2 tubulates membranes
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DOI：
10.1073/pnas.0911789106
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发表时间：
2009-12-15
影响因子：
11.1
通讯作者：
Simons, Kai
中科院分区：
文献类型：
--
作者：
Cao, Xinwang;Coskun, Unal;Simons, Kai
高尔基体相关的四磷酸衔接蛋白2（FAPP 2）已被证明具有葡萄糖神经酰胺在体外和细胞中的转移活性。我们以前已经表明，FAPP 2是参与顶端运输从高尔基复合体在上皮MDCK细胞。在本文中，我们分配一个未知的活性蛋白质，以及提供结构洞察蛋白质组装和低分辨率的包膜结构。通过应用分析超离心和小角X-射线散射，我们表明，FAPP 2是一个二聚体蛋白在溶液中，具有30 nm的长度弯曲的形状。纯化的FAPP 2蛋白具有在体外从膜片形成小管的能力。该活性依赖于FAPP 2的PH结构域的磷酸肌醇结合活性。这些数据表明，FAPP 2的功能直接在顶端载体的trans-Golgi网络的形成。
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.