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.
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Cover Image
Cover Image
Endoplasmic reticulumendosome contact sites. This pseudo-colored electron microscopy image shows the formation of inter-organelle membrane contact sites between late endosomes (magenta) and the endoplasmic reticulum (ER; green). This tethering results from the interaction between two ER-anchored proteins (VAP-A and VAP-B) and the late endosomeanchored protein STARD3NL. Mitochondria: brown; nucleus: blue. For further details see pp. 493-498. Image kindly provided by Fabien Alpy. - PDF Icon PDF LinkTable of Contents
Review Article|
April 11 2016
Touché! STARD3 and STARD3NL tether the ER to endosomes
Léa P. Wilhelm;
Léa P. Wilhelm
*Functional Genomics and Cancer Department, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), 1 rue Laurent Fries, 67404 Illkirch, France
†Institut National de la Santé et de la Recherche Médicale (INSERM), U 964, 67404 Illkirch, France
‡Centre National de la Recherche Scientifique (CNRS), UMR 7104, 67404 Illkirch, France
§Université de Strasbourg, 67404 Illkirch, France
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Catherine Tomasetto;
Catherine Tomasetto
*Functional Genomics and Cancer Department, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), 1 rue Laurent Fries, 67404 Illkirch, France
†Institut National de la Santé et de la Recherche Médicale (INSERM), U 964, 67404 Illkirch, France
‡Centre National de la Recherche Scientifique (CNRS), UMR 7104, 67404 Illkirch, France
§Université de Strasbourg, 67404 Illkirch, France
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Fabien Alpy
Fabien Alpy
1
*Functional Genomics and Cancer Department, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), 1 rue Laurent Fries, 67404 Illkirch, France
†Institut National de la Santé et de la Recherche Médicale (INSERM), U 964, 67404 Illkirch, France
‡Centre National de la Recherche Scientifique (CNRS), UMR 7104, 67404 Illkirch, France
§Université de Strasbourg, 67404 Illkirch, France
1To whom correspondence should be addressed (email Fabien.Alpy@igbmc.fr).
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Publisher: Portland Press Ltd
Received:
January 25 2016
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2016 Authors; published by Portland Press Limited
2016
Biochem Soc Trans (2016) 44 (2): 493–498.
Article history
Received:
January 25 2016
Citation
Léa P. Wilhelm, Catherine Tomasetto, Fabien Alpy; Touché! STARD3 and STARD3NL tether the ER to endosomes. Biochem Soc Trans 15 April 2016; 44 (2): 493–498. doi: https://doi.org/10.1042/BST20150269
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