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J. Biol. Chem., Vol. 277, Issue 33, 29908-29918, August 16, 2002
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From the Atlantic Research Center, Departments of Pediatrics and
Biochemistry and Molecular Biology, Dalhousie University,
Halifax, Nova Scotia B3H 4H7, Canada
Oxysterol-binding protein (OSBP) is
1 of 12 related proteins implicated in the 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 vesicle-associated membrane protein-associated protein-A
(VAP-A), a syntaxin-like protein implicated in endoplasmic reticulum
(ER)/Golgi vesicle transport, and phospholipid regulation in mammalian
cells and yeast, respectively. By using a combination of yeast
two-hybrid, glutathione S-transferase 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. C- and N-terminal
truncations or deletions of VAP prevented interaction with OSBP but did
not affect VAP multimerization. Although 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
Vesicle-associated Membrane Protein-associated Protein-A (VAP-A)
Interacts with the Oxysterol-binding Protein to Modify Export from the
Endoplasmic Reticulum*
,
132-182). OSBP W174A retained oxysterol binding
activity, association with phospholipid vesicles via the PH domain, and
localized with VAP in unusual ER-associated structures. At 40 °C,
misfolded ts045-vesicular stomatitis virus G protein fused to green
fluorescent protein was co-localized with VAP-A/OSBP W174A structures
on the ER but was exported to the Golgi when folded normally at
32 °C. 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 at a stage of protein and ceramide
transport from the ER.
*
This work was supported in part by Program Grant (to
N. D. R. and C. R. M.), Scientist (to N. D. R.), and Scholar (to
C. R. M.) awards from the Canadian Institutes of Health Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of Isaac Walton Killiam and Sumner graduate studentships.
§
To whom correspondence should be addressed: Atlantic Research
Center, Dept. of Biochemistry and Molecular Biology, Dalhousie University, 5849 University Ave., Halifax, Nova Scotia B3H 4H7, Canada.
Tel.: 902-494-7133; Fax: 902-494-1394; E-mail:
nridgway@is.dal.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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