In eukaryotic cells, a sterol gradient exists between the early and late regions of the secretory pathway. This gradient seems to rely on non-vesicular transport mechanisms mediated by specialized carriers. The oxysterol-binding protein-related protein (ORP)/oxysterol-binding homology (Osh) family has been assumed initially to exclusively include proteins acting as sterol sensors/transporters and many efforts have been made to determine their mode of action. Our recent studies have demonstrated that some ORP/Osh proteins are not mere sterol transporters, but sterol/phosphatidylinositol 4-phosphate [PI(4)P] exchangers. They exploit the PI(4)P gradient at the endoplasmic reticulum (ER)/Golgi interface, or at membrane-contact sites between these compartments, to actively create a sterol gradient. Other recent reports have suggested that all ORP/Osh proteins bind PI(4)P and recognize a second lipid that is not necessary sterol. We have thus proposed that ORP/Osh proteins use PI(4)P gradients between organelles to convey various lipid species.
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October 2014
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Conference Article|
September 18 2014
Building lipid ‘PIPelines’ throughout the cell by ORP/Osh proteins
Joachim Moser von Filseck;
Joachim Moser von Filseck
*Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France
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Bruno Mesmin;
Bruno Mesmin
*Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France
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Joëlle Bigay;
Joëlle Bigay
*Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France
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Bruno Antonny;
Bruno Antonny
*Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France
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Guillaume Drin
Guillaume Drin
1
*Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and CNRS, 660 route des lucioles, 06560 Valbonne, France
1To whom correspondence should be addressed (emaildrin@ipmc.cnrs.fr).
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Publisher: Portland Press Ltd
Received:
May 15 2014
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem Soc Trans (2014) 42 (5): 1465–1470.
Article history
Received:
May 15 2014
Citation
Joachim Moser von Filseck, Bruno Mesmin, Joëlle Bigay, Bruno Antonny, Guillaume Drin; Building lipid ‘PIPelines’ throughout the cell by ORP/Osh proteins. Biochem Soc Trans 1 October 2014; 42 (5): 1465–1470. doi: https://doi.org/10.1042/BST20140143
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