Author: 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.
Title: Proteomic Profiling of the TRAF3 Interactome Network Reveals a New Role for the ER-to-Golgi Transport Compartments in Innate Immunity Document date: 2012_7_5
ID: 1m5dbwjv_12
Snippet: Members of the TRAF family often share common interacting partners. For example, TRADD and RIP1 strongly bind to TRAF1, TRAF2 and TRAF3 [21, 35] , whereas the mitochondrial anti-viral signaling protein MAVS interacts with TRAF2, TRAF3 and TRAF6 [10, 20] . To verify the binding selectivity of the newly identified TRAF3 interactors, we next performed co-immunoprecipitation experiments in 293T cells overexpressing FLAG-tagged TRAF2, TRAF3 or TRAF6, .....
Document: Members of the TRAF family often share common interacting partners. For example, TRADD and RIP1 strongly bind to TRAF1, TRAF2 and TRAF3 [21, 35] , whereas the mitochondrial anti-viral signaling protein MAVS interacts with TRAF2, TRAF3 and TRAF6 [10, 20] . To verify the binding selectivity of the newly identified TRAF3 interactors, we next performed co-immunoprecipitation experiments in 293T cells overexpressing FLAG-tagged TRAF2, TRAF3 or TRAF6, TRAF molecules involved in type I IFN and inflammatory responses, along with Myc-p115 or EGFP-Sec16A. Only Myc-p115 was found to be enriched in FLAG-TRAF3 immunocomplexes ( Figure S1C) . A similar result was obtained with EGFP-Sec16A, except that a weak enrichment was observed with TRAF2 when compared to TRAF3 ( Figure S1D ).
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