But can signals from the Golgi lead to changes in gene expression in the nucleus? Membrane-anchored transcription factors can be released from Golgi membranes by site 1 and 2 proteases (Fox and Andrew, 2015), allowing nuclear translocation and transcription of specific genes. However, these transcription factors are trafficked to the Golgi by specific events signaled in the ER. Several golgins contain cryptic nuclear localization signals, and fragments of these proteins (generated by caspases or other proteases) can be targeted to the nucleus. But to date, none of these fragments has been shown to induce gene expression that might alter Golgi function. A caspase cleavage fragment of p115, a vesicle tethering protein localized at the cis-Golgi, is targeted to the nucleus and promotes cell death in a p53-dependent pathway (Chiu et al., 2002; How and Shields, 2011). However, cleavage of p115 is not observed in all pro-apoptotic settings (Lowe et al., 2004).