Protein disulfide isomerase-9 interacts with the lumenal region of the transmembrane endoplasmic reticulum stress sensor kinase, IRE1, to modulate the unfolded protein response in Arabidopsis

• Published in: Frontiers in plant science Vol. 15; p. 1389658
• Main Authors: Carrillo, Rina, Iwai, Kaela, Albertson, Alena, Dang, Gabrielle, Christopher, David A
• Format: Journal Article
• Language: English
• Published: Switzerland Frontiers Media S.A 16.05.2024
• Subjects: disulfide; endoplasmic reticulum stress; Plant Science; proteostasis; unfolded protein response; UPR-regulation; unfolded protein response; proteostasis; disulfide; endoplasmic reticulum stress; UPR-regulation

Environmental stressors disrupt secretory protein folding and proteostasis in the endoplasmic reticulum (ER), leading to ER stress. The unfolded protein response (UPR) senses ER stress and restores proteostasis by increasing the expression of ER-resident protein folding chaperones, such as protein d...