학술논문

ER‐to‐lysosome‐associated degradation in a nutshell: mammalian, yeast, and plant ER‐phagy as induced by misfolded proteins.
Document Type
Article
Source
FEBS Letters. Aug2023, Vol. 597 Issue 15, p1928-1945. 18p.
Subject
*PLANT proteins
*ORGANELLES
*EUKARYOTIC cells
*ENDOPLASMIC reticulum
*YEAST
*UBIQUITINATION
Language
ISSN
0014-5793
Abstract
Conserved catabolic pathways operate to remove aberrant polypeptides from the endoplasmic reticulum (ER), the major biosynthetic organelle of eukaryotic cells. The best known are the ER‐associated degradation (ERAD) pathways that control the retrotranslocation of terminally misfolded proteins across the ER membrane for clearance by the cytoplasmic ubiquitin/proteasome system. In this review, we catalog folding‐defective mammalian, yeast, and plant proteins that fail to engage ERAD machineries. We describe that they rather segregate in ER subdomains that eventually vesiculate. These ER‐derived vesicles are captured by double membrane autophagosomes, engulfed by endolysosomes/vacuoles, or fused with degradative organelles to clear cells from their toxic cargo. These client‐specific, mechanistically diverse ER‐phagy pathways are grouped under the umbrella term of ER‐to‐lysosome‐associated degradation for description in this essay. [ABSTRACT FROM AUTHOR]