The only thing Stephen King is more terrified of than giant spiders is ending his novels on a positive note. Seriously, if you remember a happy ending from a movie that had "Based on a novel by Stephen King" in the credits, chances are that's the result of some producer taking one look at the source material and saying "Oh, hell no." In Cujo , Tad's mom doesn't save the day; he dies of dehydration in the car. In Christine , the car is still out there, coming back for revenge. In Shawshank Redemption, Red rapes Andy to death. (Probably. We haven't read it.) King never wants anyone for a second to think that death isn't creeping up behind us at all times. That's why in a story where four dirt-poor kids end up getting the shit kicked out of them, they had to end up dead; otherwise, this might come off as optimistic.
As in all other eukaryotic organisms, endoplasmic reticulum (ER) stress triggers the evolutionarily conserved unfolded protein response in soybean, but it also communicates with other adaptive signaling responses, such as osmotic stress-induced and ER stress-induced programmed cell death. These two signaling pathways converge at the level of gene transcription to activate an integrated cascade that is mediated by N-rich proteins (NRPs). Here, we describe a novel transcription factor, GmERD15 (Glycine max Early Responsive to Dehydration 15), which is induced by ER stress and osmotic stress to activate the expression of NRP genes. GmERD15 was isolated because of its capacity to stably associate with the NRP-B promoter in yeast. It specifically binds to a 187-bp fragment of the NRP-B promoter in vitro and activates the transcription of a reporter gene in yeast. Furthermore, GmERD15 was found in both the cytoplasm and the nucleus, and a ChIP assay revealed that it binds to the NRP-B promoter in vivo. Expression of GmERD15 in soybean protoplasts activated the NRP-B promoter and induced expression of the NRP-B gene. Collectively, these results support the interpretation that GmERD15 functions as an upstream component of stress-induced NRP-B-mediated signaling to connect stress in the ER to an osmotic stress-induced cell death signal.