title: N-rich protein (NRP)-mediated cell death signaling: a new branch of the ER stress response with implications for plant biotechnology.
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.
authors.affiliation: Departamento de Bioquimica e Biologia Molecular, BIOAGRO, National Institute of Science and Technology in Plant-Pest Interactions, Universidade Federal de Vicosa, Vicosa, MG, Brazil.
authors.forename: Pedro A B
authors.initials: PA
authors.lastname: Reis
authors.forename: Elizabeth P B
authors.initials: EP
authors.lastname: Fontes
mesh_terms: D001709:Biotechnology; D016923:Cell Death; D059865:Endoplasmic Reticulum Stress; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D010940:Plant Proteins