Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities.

摘要: EDEM1 is a crucial regulator of endoplasmic reticulum (ER)-associated degradation (ERAD) that extracts non-native glycopolypeptides from the calnexin chaperone system. Under normal growth conditions, intralumenal level must be low to prevent premature interruption ongoing folding programs. We report in unstressed cells, segregated bulk ER into LC3-I-coated vesicles and rapidly degraded. The rapid turnover regulated by novel mechanism shows similarities but clearly distinct macroautophagy. Cells with defective contain unphysiologically high levels EDEM1, show enhanced ERAD activity are characterized impaired capacity efficiently complete maturation model glycopolypeptides. define as tuning mechanisms operating mammalian at steady state offer kinetic advantage over disposal unstructured nascent chains selective regulators.