STARD 3 mediates endoplasmic reticulum‐to‐endosome cholesterol transport at membrane contact sites - Archive ouverte HAL
Article Dans Une Revue EMBO Journal Année : 2017

STARD 3 mediates endoplasmic reticulum‐to‐endosome cholesterol transport at membrane contact sites

Résumé

StAR-related lipid transfer domain-3 (STARD3) is a sterol-binding protein that creates endoplasmic reticulum (ER)-endosome contact sites. How this protein, at the crossroad between sterol uptake and synthesis pathways, impacts the intracellular distribution of this lipid was ill-defined. Here, by using in situ cholesterol labeling and quantification, we demonstrated that STARD3 induces cholesterol accumulation in endosomes at the expense of the plasma membrane. STARD3-mediated cholesterol routing depends both on its lipid transfer activity and its ability to create ER-endosome contacts. Corroborating this, in vitro reconstitution assays indicated that STARD3 and its ER-anchored partner, Vesicle-associated membrane protein-associated protein (VAP), assemble into a machine that allows a highly efficient transport of cholesterol within membrane contacts. Thus, STARD3 is a cholesterol transporter scaffolding ER-endosome contacts and modulating cellular cholesterol repartition by delivering cholesterol to endosomes.
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hal-03409545 , version 1 (29-10-2021)

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Léa P Wilhelm, Corinne Wendling, Benoît Védie, Toshihide Kobayashi, Marie‐pierre Chenard, et al.. STARD 3 mediates endoplasmic reticulum‐to‐endosome cholesterol transport at membrane contact sites. EMBO Journal, 2017, 36 (10), pp.1412 - 1433. ⟨10.15252/embj.201695917⟩. ⟨hal-03409545⟩
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