Fiche publication
Date publication
avril 2016
Journal
Biochemical Society transactions
Auteurs
Membres identifiés du Cancéropôle Est :
Dr ALPY Fabien
,
Dr TOMASETTO Catherine
Tous les auteurs :
Wilhelm LP, Tomasetto C, Alpy F
Lien Pubmed
Résumé
Membrane contact sites (MCSs) are subcellular regions where the membranes of distinct organelles come into close apposition. These specialized areas of the cell, which are involved in inter-organelle metabolite exchange, are scaffolded by specific complexes. STARD3 [StAR (steroidogenic acute regulatory protein)-related lipid transfer domain-3] and its close paralogue STARD3NL (STARD3 N-terminal like) are involved in the formation of contacts between late-endosomes and the endoplasmic reticulum (ER). The lipid transfer protein (LTP) STARD3 and STARD3NL, which are both anchored on the limiting membrane of late endosomes (LEs), interact with ER-anchored VAP [VAMP (vesicle-associated membrane protein)-associated protein] (VAP-A and VAP-B) proteins. This direct interaction allows ER-endosome contact formation. STARD3 or STARD3NL-mediated ER-endosome contacts, which affect endosome dynamics, are believed to be involved in cholesterol transport.
Mots clés
Binding Sites, Biological Transport, Carrier Proteins, metabolism, Cholesterol, metabolism, Endoplasmic Reticulum, metabolism, Endosomes, metabolism, Humans, Membrane Proteins, metabolism, Protein Binding
Référence
Biochem. Soc. Trans.. 2016 Apr;44(2):493-8
