Endoplasmic reticulum oxidoreductase 1 alpha (ERO1A)

Endoplasmic reticulum oxidoreductase 1 alpha (ERO1A) is a flavoprotein enzyme that catalyzes the formation of disulfide bonds in newly synthesized proteins within the endoplasmic reticulum (ER)[1][3]. It interacts with protein disulfide isomerase (PDI), efficiently reoxidizing it to promote continued disulfide bond formation necessary for proper protein folding[2][3]. ERO1A uses flavin adenine dinucleotide (FAD) as a cofactor to transfer electrons from PDI to molecular oxygen, generating reactive oxygen species (ROS) as a byproduct[2][3]. Overexpression or dysregulation of ERO1A is associated with poor prognosis and aggressive cancer phenotypes, as it supports tumor cell adaptation to hypoxia, promotes angiogenesis, and is implicated in immune escape by regulating protein folding in secretory pathways critical for tumor progression[1][4]. ERO1A has emerged as a promising therapeutic target in oncology and is under investigation for small molecule inhibitors[4].

Other names

ERO1-like protein alphaERO1LUNQ434/PRO865ERO1-LERO1-L-alphaERO1-alphaEro1alphaEndoplasmic oxidoreductin-1-like proteinEndoplasmic reticulum oxidoreductase alphaOxidoreductin-1-L-alphaERO1LA

Inhibition of ERO1A disrupts oxidative protein folding, impairs disulfide bond formation, leads to ER stress, and could promote apoptosis in cancer cells.