PMC:4635215 / 9032-10274 JSONTXT

{"project":"TEST0","denotations":[{"id":"26594142-203-211-125968","span":{"begin":203,"end":207},"obj":"[\"12130652\"]"},{"id":"26594142-184-192-125969","span":{"begin":394,"end":398},"obj":"[\"15979510\"]"},{"id":"26594142-86-94-125970","span":{"begin":806,"end":810},"obj":"[\"15829563\"]"}],"text":"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."}

{"project":"0_colil","denotations":[{"id":"26594142-12130652-125968","span":{"begin":203,"end":207},"obj":"12130652"},{"id":"26594142-15979510-125969","span":{"begin":394,"end":398},"obj":"15979510"},{"id":"26594142-15829563-125970","span":{"begin":806,"end":810},"obj":"15829563"}],"text":"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."}

{"project":"2_test","denotations":[{"id":"26594142-12130652-38084440","span":{"begin":203,"end":207},"obj":"12130652"},{"id":"26594142-15979510-38084441","span":{"begin":394,"end":398},"obj":"15979510"},{"id":"26594142-15829563-38084442","span":{"begin":806,"end":810},"obj":"15829563"}],"text":"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."}