PT  - JOURNAL ARTICLE
AU  - Alpy, Fabien
AU  - Rousseau, Adrien
AU  - Schwab, Yannick
AU  - Legueux, François
AU  - Stoll, Isabelle
AU  - Wendling, Corinne
AU  - Spiegelhalter, Coralie
AU  - Kessler, Pascal
AU  - Mathelin, Carole
AU  - Rio, Marie-Christine
AU  - Levine, Timothy P.
AU  - Tomasetto, Catherine
TI  - STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER
AID  - 10.1242/jcs.139295
DP  - 2013 Dec 01
TA  - Journal of Cell Science
PG  - 5500--5512
VI  - 126
IP  - 23
4099  - http://jcs.biologists.org/content/126/23/5500.short
4100  - http://jcs.biologists.org/content/126/23/5500.full
SO  - J. Cell Sci.2013 Dec 01; 126
AB  - Inter-organelle membrane contacts sites (MCSs) are specific subcellular regions favoring the exchange of metabolites and information. We investigated the potential role of the late-endosomal membrane-anchored proteins StAR related lipid transfer domain-3 (STARD3) and STARD3 N-terminal like (STARD3NL) in the formation of MCSs involving late-endosomes (LEs). We demonstrate that both STARD3 and STARD3NL create MCSs between LEs and the endoplasmic reticulum (ER). STARD3 and STARD3NL use a conserved two phenylalanines in an acidic tract (FFAT)-motif to interact with ER-anchored VAP proteins. Together, they form an LE–ER tethering complex allowing heterologous membrane apposition. This LE–ER tethering complex affects organelle dynamics by altering the formation of endosomal tubules. An in situ proximity ligation assay between STARD3, STARD3NL and VAP proteins identified endogenous LE–ER MCS. Thus, we report here the identification of proteins involved in inter-organellar interaction.