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Vol. 12, Issue 6, 1633-1644, June 2001
and
MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, United
Kingdom
Oxysterol binding protein (OSBP) is the only protein known to bind
specifically to the group of oxysterols with potent effects on
cholesterol homeostasis. Although the function of OSBP is currently unknown, an important role is implicated by the existence of multiple homologues in all eukaryotes so far examined. OSBP and a subset of
homologues contain pleckstrin homology (PH) domains. Such domains are
responsible for the targeting of a wide range of proteins to the plasma
membrane. In contrast, OSBP is a peripheral protein of Golgi membranes,
and its PH domain targets to the trans-Golgi network of mammalian cells. In this article, we have
characterized Osh1p, Osh2p, and Osh3p, the three homologues of OSBP in
Saccharomyces cerevisiae that contain PH domains.
Examination of a green fluorescent protein (GFP) fusion to Osh1p
revealed a striking dual localization with the protein present on both
the late Golgi, and in the recently described nucleus-vacuole (NV)
junction. Deletion mapping revealed that the PH domain of Osh1p
specified targeting to the late Golgi, and an ankyrin repeat domain
targeting to the NV junction, the first such targeting domain
identified for this structure. GFP fusions to Osh2p and Osh3p showed
intracellular distributions distinct from that of Osh1p, and their PH
domains appear to contribute to their differing localizations.
Present address: Department of Cell
Biology, Institute of Opthalmology, 11-43 Bath Street, London EC1V 9EL,
United Kingdom.
*
Corresponding author. E-mail address:
sean{at}mrc-lmb.cam.ac.uk.
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