Golgi protein FAPP2 tubulates membranes

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Xinwang Cao - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Ünal Coskun - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Manfred Rössle - , European Molecular Biology Laboratory (EMBL) Heidelberg (Author)
  • Sabine B. Buschhorn - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Michal Grzybek - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Timothy R. Dafforn - , University of Birmingham (Author)
  • Marc Lenoir - , University of Birmingham (Author)
  • Michael Overduin - , University of Birmingham (Author)
  • Kai Simons - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)

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
JournalProceedings of the National Academy of Sciences of the United States of America : PNAS
Volume106
Issue number50
Publication statusPublished - 15 Dec 2009
Peer-reviewedYes
Externally publishedYes

External IDs

WOS 000272795300022
Scopus 75849125878
ORCID /0000-0003-2083-0506/work/148607250

Keywords

ASJC Scopus subject areas

Keywords

  • Membrane tubulation, PH domain, Phosphatidylinositol 4-phosphate, Small-angle x-ray scattering (SAXS), Trans-Golgi network

Library keywords