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- W2793234310 endingPage "3345" @default.
- W2793234310 startingPage "3333" @default.
- W2793234310 abstract "Secretory proteins undergo modifications such as glycosylation and disulphide bond formation before proper folding, and move to their final destination via the endomembrane system. Accumulation of unfolded proteins in the endoplasmic reticulum (ER) due to suboptimal environmental conditions triggers a response called the unfolded protein response (UPR), which induces a set of genes that elevate protein folding capacity in the ER. This review aims to establish a connection among ER stress, UPR, and reactive oxygen species (ROS), which remains an unexplored topic in plants. For this, we focused on mechanisms of ROS production originating from ER stress, the interaction between ER stress and overall ROS signalling process in the cell, and the interaction of ER stress with other organellar ROS signalling pathways such as of the mitochondria and chloroplasts. The roles of the UPR during plant hormone signalling and abiotic and biotic stress responses are also discussed in connection with redox and ROS signalling." @default.
- W2793234310 created "2018-03-29" @default.
- W2793234310 creator A5035223994 @default.
- W2793234310 creator A5043850734 @default.
- W2793234310 creator A5052276041 @default.
- W2793234310 creator A5078755481 @default.
- W2793234310 creator A5091651970 @default.
- W2793234310 date "2018-02-28" @default.
- W2793234310 modified "2023-10-01" @default.
- W2793234310 title "Interplay between the unfolded protein response and reactive oxygen species: a dynamic duo" @default.
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