Unknown

Dataset Information

0

A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation.

ABSTRACT: 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.

SUBMITTER: Cui Y 

PROVIDER: S-EPMC7062386 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

A COPII subunit acts with an autophagy receptor to target endoplasmic reticulum for degradation.

Cui Yixian Y   Parashar Smriti S   Zahoor Muhammad M   Needham Patrick G PG   Mari Muriel M   Zhu Ming M   Chen Shuliang S   Ho Hsuan-Chung HC   Reggiori Fulvio F   Farhan Hesso H   Brodsky Jeffrey L JL   Ferro-Novick Susan S  

Science (New York, N.Y.) 20190701 6448

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  ...[more]

Similar Datasets

Unknown Interplay between Endoplasmic Reticulum (ER) Stress and Autophagy Induces Mutant p53H273 Degradation.
| S-EPMC7175121 | biostudies-literature
Unknown ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery.
| S-EPMC4163648 | biostudies-literature
Transcriptomics IRE1alpha is an endogenous substrate of endoplasmic reticulum-associated degradation
2015-11-04 | E-GEOD-70563 | biostudies-arrayexpress
Unknown Sel1L is indispensable for mammalian endoplasmic reticulum-associated degradation, endoplasmic reticulum homeostasis, and survival.
| S-EPMC3918815 | biostudies-literature
Unknown TorsinA participates in endoplasmic reticulum-associated degradation.
| S-EPMC3529909 | biostudies-literature
Unknown HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation.
| S-EPMC3033308 | biostudies-literature
Transcriptomics Tunicamycin-induced Endoplasmic Reticulum-Quality Control Pathway and Endoplasmic Reticulum-Associated Degradation Mechanism in the diatom Phaeodactylum tricornutum
2022-08-02 | GSE209809 | GEO
Unknown Conserved endoplasmic reticulum-associated degradation system to eliminate mutated receptor-like kinases in Arabidopsis.
| S-EPMC3021050 | biostudies-literature
Unknown Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways.
| S-EPMC6926463 | biostudies-literature
Unknown Atlastins remodel the endoplasmic reticulum for selective autophagy.
| S-EPMC6168278 | biostudies-literature