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• W2024248082 abstract "Upon disruption of ER homeostasis, plant cells activate at least two branches of the unfolded protein response (UPR) through IRE1-like and ATAF6-like transducers, resulting in the upregulation of ER-resident molecular chaperones and the activation of the ER-associated degradation protein system. Here, we discuss a new ER stress response pathway in plants that is associated with an osmotic stress response in transducing a cell death signal. Both ER and osmotic stress induce the expression of the novel transcription factor GmERD15, which binds and activates N-rich protein (NRP) promoters to induce NRP expression and cause the upregulation of GmNAC6, an effector of the cell death response. In contrast to this activation mechanism, the ER-resident molecular chaperone binding protein (BiP) attenuates the propagation of the cell death signal by modulating the expression and activity of components of the ER and osmotic stress-induced NRP-mediated cell death signaling. This interaction attenuates dehydration-induced cell death and promotes a better adaptation of BiP-overexpressing transgenic lines to drought." @default.
• W2024248082 created "2016-06-24" @default.
• W2024248082 creator A5052641740 @default.
• W2024248082 creator A5053543995 @default.
• W2024248082 date "2012-06-01" @default.
• W2024248082 modified "2023-09-26" @default.
• W2024248082 title "N-rich protein (NRP)-mediated cell death signaling" @default.
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• W2024248082 doi "https://doi.org/10.4161/psb.20111" @default.
• W2024248082 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3442856" @default.
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