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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Golgi protein FAPP2 tubulates membranes.
Proc. Natl. Acad. Sci. U.S.A. 106, 21121-21125 (2009)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
2009
HGF-reported in Year
0
ISSN (print) / ISBN
0027-8424
e-ISSN
1091-6490
Quellenangaben
Volume: 106,
Issue: 50,
Pages: 21121-21125
Publisher
National Academy of Sciences
Reviewing status
Peer reviewed
Institute(s)
Institute of Pancreatic Islet Research (IPI)
PubMed ID
19940249
Erfassungsdatum
2009-12-31