Open AccessA COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation
Author(s) -
Yixian Cui,
Smriti Parashar,
Muhammad Zahoor,
Patrick G. Needham,
Muriel Mari,
Ming Zhu,
Shuliang Chen,
Hsuan-Chung Ho,
Fulvio Reggiori,
Hesso Farhan,
Jeffrey L. Brodsky,
Susan FerroNovick
Publication year - 2019
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aau9263
Subject(s) - endoplasmic reticulum , copii , microbiology and biotechnology , golgi apparatus , autophagy , copi , secretory pathway , endoplasmic reticulum associated protein degradation , secretory protein , protein subunit , receptor , unfolded protein response , chemistry , biology , secretion , biochemistry , gene , apoptosis
The COPII-cargo adaptor complex Lst1-Sec23 selectively sorts proteins into vesicles that bud from the endoplasmic reticulum (ER) and traffic to the Golgi. Improperly folded proteins are prevented from exiting the ER and are degraded. ER-phagy is an autophagic degradation pathway that uses ER-resident receptors. Working in yeast, we found an unexpected role for Lst1-Sec23 in ER-phagy that was independent from its function in secretion. Up-regulation of the stress-inducible ER-phagy receptor Atg40 induced the association of Lst1-Sec23 with Atg40 at distinct ER domains to package ER into autophagosomes. Lst1-mediated ER-phagy played a vital role in maintaining cellular homeostasis by preventing the accumulation of an aggregation-prone protein in the ER. Lst1 function appears to be conserved because its mammalian homolog, SEC24C, was also required for ER-phagy.
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