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.