Golgi protein FAPP2 tubulates membranes

Research output: Contribution to journalArticle

Authors

  • X Cao
  • U Coskun
  • M Rossle
  • SB Buschhorn
  • M Grzybek
  • K Simons

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.

Details

Original languageEnglish
Pages (from-to)21121-21125
Number of pages5
JournalNational Academy of Sciences. Proceedings
Volume106
Issue number50
Publication statusPublished - 25 Nov 2009

Keywords

  • HLA immunogenicity, phosphatidylinositol 4-phosphate, PH domain, Hydrophobicity, trans-Golgi network, membrane tubulation, small-angle x-ray scattering (SAXS), Electrostatic charge