We previously reported that procaspase-2 is partially localized at the cytoplasmic face of the Golgi complex (Mancini et al., 2000), and golgin-160 and several other golgins are caspase-2 substrates (Mancini et al., 2000; Lowe et al., 2004). Caspase cleavage of golgin-160 is predicted to inhibit its function in promoting efficient trafficking of specific cargo molecules (Bundis et al., 2006; Hicks et al., 2006; Williams et al., 2006). Caspase-2 is an unusual caspase in that it possesses a long prodomain like inititator caspases, but does not activate effector caspases (Fava et al., 2012). Recent evidence suggests non-apoptotic roles for caspase-2 in maintaining genome stability, checkpoint regulation in the cell cycle, response to oxidative stress, tumor suppression and in aging (Olsson et al., 2015).