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Reticulon proteins modulate autophagy of the endoplasmic reticulum in maize endosperm

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TLDR
It is proposed that maize Rtn1 and Rtn2 act as receptors for autophagy-mediated ER turnover, and thus are critical for ER homeostasis and suppression of ER stress.
Abstract
Reticulon (Rtn) proteins shape tubular domains of the endoplasmic reticulum (ER), and in some cases are autophagy receptors for selective ER turnover. We have found that maize Rtn1 and Rtn2 control ER homeostasis and autophagic flux in endosperm aleurone cells, where the ER accumulates lipid droplets and synthesizes storage protein accretions metabolized during germination. Maize Rtn1 and Rtn2 are expressed in the endosperm, localize to the ER, and re-model ER architecture in a dose-dependent manner. Rtn1 and Rtn2 interact with Atg8a using four Atg8-interacting motifs (AIMs) located at the C-terminus, cytoplasmic loop, and within the transmembrane segments. Binding between Rtn2 and Atg8 is elevated upon ER stress. Maize rtn2 mutants display increased autophagy and up-regulation of an ER stress-responsive chaperone. We propose that maize Rtn1 and Rtn2 act as receptors for autophagy-mediated ER turnover, and thus are critical for ER homeostasis and suppression of ER stress.

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비만과 ER Stress

TL;DR: Endoplastic reticulum (ER) as discussed by the authors folding, lipid, sterol, and protein response (UPR) are proteins that fold, fold, and fold, respectively.
Journal ArticleDOI

Protein Quality Control in Plant Organelles: Current Progress and Future Perspectives.

TL;DR: Recent progress in understanding of protein quality control in the ER, chloroplasts, and mitochondria in plants is summarized, with a focus on the common mechanisms shared in these organelles during protein homeostasis.
Journal ArticleDOI

ER-phagy responses in yeast, plants, and mammalian cells and their crosstalk with UPR and ERAD.

TL;DR: The concept of ER-phagy responses (ERPRs) was introduced in this paper. ERPRs ensure lysosomal clearance of ER portions expendable during nutrient shortage, nonfunctional, present in excess, or containing misfolded proteins.
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