EDEM1 (ER degradation enhancing alpha-mannosidase like protein 1) is a glycosyl hydrolase 47 family member that serves as a critical quality control factor in endoplasmic reticulum-associated degradation (ERAD) 1. Its primary function is extracting misfolded N-glycosylated proteins from the calnexin chaperone cycle for proteasomal degradation, while permitting productive protein folding to proceed 2. Mechanistically, EDEM1 catalyzes α1,2-mannose trimming of N-glycans, converting Man8GlcNAc2 to Man7GlcNAc2 and generating oligosaccharide structures (M7, M6, M5) that mark proteins for degradation 3. This mannose-trimming activity operates in both ERAD-dependent and independent pathways, often coordinating with the SEL1L/Hrd1 complex 4. EDEM1 protein levels are dynamically regulated through both ERAD and autophagy during ER stress 4. Disease relevance extends to conditions involving ER stress and protein misfolding; notably, EDEM1 alterations enhance ATF6 pro-survival signaling in hepatocellular carcinoma cells 5, and EDEM1 expression is upregulated in response to chemical stressors like PFAS-induced toxicity 6. Clinically, understanding EDEM1 function informs therapeutic strategies targeting ER stress-related pathologies and may have implications for viral infections that manipulate ER quality control mechanisms.