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Med Sci (Paris). 2020 Feb;36(2):130-136. doi: 10.1051/medsci/2020009. Epub 2020 Mar 4.

[A lipid exchange market : vectorial cholesterol transport by the protein OSBP].

[Article in French; Abstract available in French from the publisher]

Author information

1
Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur et CNRS, UMR 7275, 660 route des lucioles, 06560 Valbonne, France.

Abstract

in English, French

Cholesterol is synthesized in the endoplasmic reticulum (RE) and then transported to cellular compartments whose functions require high cholesterol levels. Here, we describe the mechanism by which cholesterol is transported from the RE to the trans-Golgi network (TGN) by the protein OSBP (Oxysterol-Binding Protein). OSBP has two complementary activities. First, it tethers the RE to the TGN by forming a contact site where the two membranes are about twenty nanometers away. Then, it exchanges RE cholesterol for a TGN lipid, phosphatidylinositol 4-phosphate (PI4P). Eventually, PI4P is hydrolyzed at the RE, making the exchange cycle irreversible. Thus, OSBP is at the center of a lipid exchange market where a transported cholesterol "costs" a PI4P. Antiviral or anti-cancer molecules target OSBP, suggesting the importance of the OSBP cycle in different physiopathological contexts. The general principles of this cycle are shared by other lipid-transfer proteins.

PMID:
32129748
DOI:
10.1051/medsci/2020009

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