Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling |
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Authors: | G D Fairn C R McMaster |
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Institution: | (1) Departments of Pediatrics and Biochemistry & Molecular Biology, Atlantic Research Centre, Dalhousie University, B3H 4H7 Nova Scotia, Canada |
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Abstract: | OSBP (oxysterol-binding protein) and ORPs (OSBP-related proteins) constitute an enigmatic eukaryotic protein family that is
united by a signature domain that binds oxysterols, sterols, and possibly other hydrophobic ligands. The human genome contains
12 OSBP/ORP family members genes, while that of the budding yeast Saccharomyces cerevisiae encodes seven OSBP homologues (Osh). Of these, Osh4 (also referred to as Kes1) has been the most widely studied to date.
Recently, three-dimensional crystal structures of Osh4 with and without sterols bound within the core of the protein were
determined. The core consists of 19 anti-parallel β-sheets that form a near-complete β-barrel. Recent work has suggested that
Osh proteins facilitate the non-vesicular transport of sterols in vivo and in vitro, while other evidence supports a role for Osh proteins in the regulation of vesicular transport and lipid metabolism.This
article will review recent advances in the study of ORP/Osh proteins and will discuss future research issues regarding the
ORP/Osh family.
Received 17 July 2007; received after revision 14 August 2007; accepted 12 September 2007 |
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Keywords: | Oxysterol-binding protein sterol phospholipid vesicular transport nonvesicular transport |
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