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MBC in Press, published online ahead of print March 29, 2006
Mol. Biol. Cell 10.1091/mbc.E06-01-0060

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Submitted on January 23, 2006
Revised on March 2, 2006
Accepted on March 22, 2006

Oxysterol-binding Protein and VAMP-associated Protein Are Required for Sterol-dependent Activation of the Ceramide Transport Protein

Ryan J. Perry and Neale D. Ridgway

Atlantic Research Centre, Departments of Pediatrics and Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7

Monitoring Editor: Sean Munro

Sphingomyelin (SM) and cholesterol are coregulated metabolically and associate physically in membrane microdomains involved in cargo sorting and signaling. One mechanism for regulation of this metabolic interface involves oxysterol binding protein (OSBP) via high-affinity binding to oxysterol regulators of cholesterol homeostasis and activation of SM synthesis at the Golgi apparatus. Here we show that OSBP regulation of SM synthesis involves the ER-to-Golgi ceramide transport protein (CERT). RNA interference (RNAi) experiments in CHO-K1 cells revealed that OSBP and vesicle-associated membrane protein-associated protein (VAP) were required for stimulation of CERT-dependent ceramide transport and SM synthesis by 25-hydroxycholesterol and cholesterol depletion in response to cyclodextrin. Additional RNAi experiments in HEK293 cells supported OSBP involvement in oxysterol-activated SM synthesis and also revealed a role for OSBP in basal SM synthesis. Activation of ER-to-Golgi ceramide transport in CHO-K1 cells required interaction of OSBP with the ER and Golgi apparatus, OSBP-dependent Golgi translocation of CERT and enhanced CERT-VAP interaction. Regulation of CERT by OSBP, sterols and VAP reveals a novel mechanism for integrating sterol regulatory signals with ceramide transport and SM synthesis in the Golgi apparatus.

Address correspondence to: Neale D. Ridgway (nridgway{at}dal.ca)




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