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PLoS One. 2013 Nov 18;8(11):e80470. doi: 10.1371/journal.pone.0080470. eCollection 2013.

SUMOylation is required for optimal TRAF3 signaling capacity.

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Molecular and Cellular Biology Laboratory, University of Crete School of Medicine, Heraklion, Greece ; Laboratory of Cancer Biology, Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology Hellas, Heraklion, Greece.


TNF receptor-associated factors (TRAFs) are multifunctional adaptor proteins involved in temporal and spatial coordination of signals necessary for normal immune function. Here, we report that TRAF3, a TRAF family member with a key role in Toll-like and TNF family receptor signaling and suppressor of lymphomagenesis, is post-translationally modified by the small ubiquitin-related modifier (SUMO). Through yeast two-hybrid and co-immunoprecipitation assays we have identified Ubc9, the SUMO conjugating enzyme, as a novel TRAF3-interacting protein. We show that Ubc9-dependent SUMOylation of TRAF3 modulates optimal association with the CD40 receptor, thereby influencing TRAF3 degradation and non-canonical NF-κB activation upon CD40 triggering. Collectively, our findings describe a novel post-translational modification of a TRAF family member and reveal a link between SUMOylation and TRAF-mediated signal transduction.

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