guest ::
| Home > Publications database > Golgi protein FAPP2 tubulates membranes |
| Home > Publications database > Golgi protein FAPP2 tubulates membranes |
| Journal Article | PHPPUBDB-12319 |
; ; ; ; ; ; ; ; ;
2009
Academy
Washington, DC
This record in other databases: 
Please use a persistent id in citations: doi:10.1073/pnas.0911789106
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.
Keyword(s): Adaptor Proteins, Signal Transducing: chemistry (MeSH) ; Adaptor Proteins, Signal Transducing: metabolism (MeSH) ; Adaptor Proteins, Signal Transducing: physiology (MeSH) ; Animals (MeSH) ; Cell Line (MeSH) ; Dogs (MeSH) ; Lipid Bilayers: metabolism (MeSH) ; Phosphatidylinositols: metabolism (MeSH) ; Protein Binding (MeSH) ; Protein Conformation (MeSH) ; Protein Multimerization (MeSH) ; Solutions (MeSH) ; trans-Golgi Network (MeSH) ; Adaptor Proteins, Signal Transducing ; Lipid Bilayers ; PLEKHA8 protein, human ; Phosphatidylinositols ; Solutions
; 
; JCR ; No Author Disambiguation ; Thomson Reuters Master Journal List ; Web of Science Core Collection
|
The record appears in these collections: |
ZIP