Proteomic Profiling of the TRAF3 Interactome Network Reveals a New Role for the ER-to-Golgi Transport Compartments in Innate Immunity

van Zuylen, Wendy J.; Doyon, Priscilla; Clément, Jean-François; Khan, Kashif Aziz; D'Ambrosio, Lisa M.; Dô, Florence; St-Amant-Verret, Myriam; Wissanji, Tasheen; Emery, Gregory; Gingras, Anne-Claude; Meloche, Sylvain; Servant, Marc J.

The notion of cellular proximity to favor exchanges and signalling events between organelles has been an intense field of interest for many years. Recently, mitofusin 2 present on the ER was shown to tether the ER to mitochondria in order to promote efficient Ca 2+ uptake into the mitochondria for oxidative phosphorylation purposes. Interestingly, mitofusin 2 was also shown to inhibit RLH pathway signalling by interacting with the C-terminal of MAVS [70] . Furthermore, the Golgi localization of the glycolipid GD3 is important for its transport to the mitochondria after TNF-a stimulation [71, 72] . Membrane scrambling between Golgi and mitochondria following Fas stimulation is another example pointing to the connection between different cellular organelles [73] . Moreover, signalling at the Golgi apparatus and endosomes has been observed for different types of membranebound receptors [56, 74] and protein kinase cascades [75] .