Abstract
The endoplasmic reticulum (ER) is the starting point for protein secretion and lipid biosynthesis in eukaryotes. ER homeostasis is precisely regulated by the unfolded protein response (UPR) to alleviate stress, involving both transcriptional and translational regulators. Autophagy is an intracellular self-eating process mediated by the double-membrane structure autophagosome for the degradation of cytosolic components and damaged organelles to regenerate nutrient supplies under nutrient-deficient or stress conditions. A recent study has revealed that besides serving as a membrane source for phagophore formation, the ER is also tightly regulated under stress conditions by a distinct type of autophagosome, namely ER-phagy. ER-phagy has been characterized with receptors clearly identified in mammals and yeast, yet relatively little is known about plant ER-phagy and its receptors. Here, we will summarize our current knowledge of ER-phagy in yeast and mammals and highlight recent progress in plant ER-phagy studies, pointing towards a possible interplay between ER-phagy and ER homeostasis under ER stress responses (ERSRs) in plants.
Highlights
Reviewed by: Giovanni Stefano, Michigan State University, United States Hadas Zehavi, Weizmann Institute of Science, Israel
We will summarize our current knowledge of endoplasmic reticulum (ER)-phagy in yeast and mammals and highlight recent progress in plant ER-phagy studies, pointing towards a possible interplay between ER-phagy and ER homeostasis under ER stress responses (ERSRs) in plants
In tissues with a high secretory activity or under adverse environmental conditions, the demands on protein folding can exceed the capacity of the ER quality control (ERQC) and ER-associated degradation (ERAD) systems, causing misfolded or unfolded protein to accumulate in the ER and eventually leading to ER stress in plants
Summary
Plant ER-phagy and ER stress mRNA encoding Hac1, the transcription factor activating the expression of ER stress response (ERSR) genes in yeast (Ron and Walter, 2007) (Table 1). The spliced bZIP60 mRNA is translated and activates the ER chaperone binding protein BiP3, triggering downstream UPRs in order to regulate ERSR (Deng et al, 2011; Nagashima et al, 2011) (Table 1).
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