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Papers In Press, published online ahead of print May 21, 2002
Biochemistry and Pediatrics, Dalhousie University, Halifax, Nova Scotia B3H 4H7
Corresponding Author: nridgway{at}is.dal.ca
Oxysterol binding protein (OSBP) is one of twelve related proteins implicated in regulation of vesicle transport and sterol homeostasis. A yeast two-hybrid screen using full-length OSBP as bait was undertaken to identify partner proteins that would provide clues to the function of OSBP. This resulted in the cloning of VAMP-associated protein-A (VAP-A), a syntaxin-like protein implicated in ER/Golgi vesicle transport and phospholipid regulation in mammalian cells and yeast, respectively. Using a combination of yeast-two hybrid, GST-pull down and immunoprecipitation experiments, the VAP-A binding region in OSBP was localized to amino acids 351-442. This region did not include the pleckstrin homology (PH) domain but overlapped with the N-terminus of the oxysterol binding and OSBP homology domains. The OSBP-binding region of VAP-A was localized to the N-terminal 160 amino acids and was independent of VAP-A multimerization. While the OSBP PH domain was not necessary for VAP-A binding in vitro, interaction with VAP-A was enhanced in cells by mutation of the conserved PH domain tryptophan (OSBP W174A) or deletion of the C-terminal half of the PH domain (OSBP
J. Biol. Chem, 10.1074/jbc.M201191200
Submitted on February 5, 2002
Revised on May 20, 2002
Accepted on May 20, 2002
VAMP-associated protein-A (VAP-A) interacts with the oxysterol binding protein (OSBP) to modify export from the endoplasmic reticulum
132-182). OSBP W174A retained oxysterol binding activity, and association with phospholipid vesicles via the PH domain, and localized with VAP in unusual ER-associated structures. At 40oC, misfolded ts045-vesicular stomatitus virus G protein fused to green fluorescent protein (VSVG-GFP) was co-localized with VAP-A/OSBP W174A structures on the ER but was exported to the Golgi when folded normally at 32oC. A fluorescent ceramide analogue also accumulated in these ER inclusions, and export to the Golgi was partially inhibited as indicated by decreased Golgi staining and a 30% reduction in sphingomyelin synthesis. These studies show that OSBP binding to the ER and Golgi apparatus is regulated by its PH domain and VAP interactions, and the complex is involved in a unidentified stage of protein and ceramide transport.
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