A cryptic nuclear localization signal is present in a fragment of golgin-160 generated by caspase-2 cleavage, and this fragment accumulates in the nucleus when expressed exogenously (Hicks and Machamer, 2002). We hypothesized that Golgi stress leads to low levels of caspase-2 activation, and that the nuclear fragments of golgin-160 participate in a stress repair pathway (Hicks and Machamer, 2005). The nuclear fragments do not resemble transcription factors per se, so may serve as transcriptional enhancers or repressors. Interestingly, cells expressing caspase-resistant golgin-160 were less sensitive to apoptosis induced by ER stress and death receptor ligation compared to cells expressing wild-type golgin-160. However, these cells responded normally to other pro-apoptotic stresses (Maag et al., 2005). Our recent data support the idea that the stable lines expressing caspase-resistant golgin-160 adapted during selection because a block in golgin-160 cleavage prevented normal response to stress. Although it is interesting that only stress within the secretory pathway depends on golgin-160 cleavage, we still lack direct evidence that golgin-160 is cleaved during Golgi stress and mediates subsequent changes in gene expression.