文章基本信息

标题：Golgi protein FAPP2 tubulates membranes
本地全文：下载
作者：Xinwang Cao ; Ünal Coskun ; Manfred Rössle 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2009
卷号：106
期号：50
页码：21121-21125
DOI：10.1073/pnas.0911789106
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
关键词：membrane tubulation ; PH domain ; phosphatidylinositol 4-phosphate ; trans-Golgi network ; small-angle x-ray scattering (SAXS)