A selective ER-phagy exerts procollagen quality control via a CALNEXIN-FAM134B complex

ABSTRACT: Autophagy is a cytosolic quality control process that recognizes substrates through receptor-mediated mechanisms. Procollagens, the most abundant gene products in metazoa, are synthesized in the endoplasmic reticulum (ER), and a fraction that fails to attain the native structure is cleared by autophagy. However, how autophagy selectively recognizes misfolded procollagens in the ER lumen is still unknown. We performed siRNA interference, CRISPR-Cas9 or knockout-mediated gene deletion of candidate autophagy and ER proteins in collagen producing cells. We found that the ER-resident lectin chaperone CALNEXIN (CANX) and the ER-phagy receptor FAM134B are required for autophagy-mediated quality control of endogenous procollagens. Mechanistically, CANX acts as co-receptor that recognizes ER-lumina

SUBMITTER: Alison Forrester 

PROVIDER: S-SCDT-EMBOJ-2018-99847 | biostudies-other |

REPOSITORIES: biostudies-other