Figure 1.

Ahn et al. identify Nogo-B as a novel modulator of interferon signaling. Activated Ras caused pronounced proteasome-dependent Nogo-B cleavage (ER-bound Nogo-B is depicted in this schematic that is likely also applicable to plasma membrane-bound Nogo-B).  Both full-length and cleaved Nogo-B contributed to reduced interferon signaling, with cleaved Nogo-B having more potent inhibitory effects. Nogo-B regulated interferon suppression occurred independent of the well-implicated Ras/MEK/ERK pathway. Detailed mechanistic links between Ras, Nogo-B, and IFN remain to be established.