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Oxysterol-Binding Proteins

  • Neale D. RidgwayEmail author
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 51)

Abstract

In eukaryotic cells, membranes of the late secretory pathway contain a disproportionally large amount of cholesterol in relation to the endoplasmic reticulum, nuclear envelope and mitochondria. At one extreme, enrichment of the plasma membrane with cholesterol and sphingolipids is crucial for formation of liquid ordered domains (rafts) involved in cell communication and transport. On the other hand, regulatory machinery in the endoplasmic reticulum is maintained in a relatively cholesterol-poor environment, to ensure appropriate rapid responses to fluctuations in cellular sterol levels. Thus, cholesterol homeostasis is absolutely dependent on its distribution along an intracellular gradient. It is apparent that this gradient is maintained by a combination of sterol-lipid interactions, vesicular transport and sterol-binding/transport proteins. Evidence for rapid, energy-independent transport between organelles has implicated transport proteins, in particular the eukaryotic oxysterol binding protein (OSBP) family. Since the founding member of this family was identified more than 25 years ago, accumulated evidence implicates the 12-member family of OSBP and OSBP-related proteins (ORPs) in sterol signalling and/or sterol transport functions. The OSBP/ORP gene family is characterized by a conserved β-barrel sterol-binding fold but is differentiated from other sterol-binding proteins by the presence of additional domains that target multiple organelle membranes. Here we will discuss the functional and structural characteristics of the mammalian OSBP/ORP family that support a ‘dual-targeting’ model for sterol transport between membranes.

Keywords

Cholesterol Endoplasmic reticulum Golgi apparatus Oxysterols Sterol transport 

Abbreviations

ABC

ATP-binding cassette

ACAT

acyl-CoA:cholesterol acyltransferase

APP

amyloid precursor protein

CERT

ceramide transfer protein

ER

endoplasmic reticulum

FFAT

two phenylalanines in an acidic tract

LDL

low density lipoprotein

LXR

liver X receptor

NPC

Niemann-Pick C

OHD

OSBP-homology domain

OSBP

oxysterol binding protein

ORP

OSBP-related protein

NVJ

nuclear-vacuolar junction

PDK

phosphoinositide-dependent kinase

PIP

phosphatidylinositol phosphate

PI4P

phosphatidylinositol 4-phosphate

PI4, 5P2

phosphatidylinositol 4,5-bisphosphate

PH

pleckstrin homology

PM

plasma membrane

PP2A

protein phosphatase 2A

RNAi

RNA interference

SREBP

sterol-regulatory element binding protein

SM

sphingomyelin

START

steroidogenic acute regulatory transport

VAP

vesicle-associated membrane protein-associated protein

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© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Departments of Pediatrics and Biochemistry & Molecular BiologyAtlantic Research Centre, Dalhousie UniversityNova ScotiaCanada

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