Calnexin (CNX), an abundant ~90 kDa molecular chaperone, is a resident type I transmembrane protein of the endoplasmic reticulum (ER) (ref.1,2). A majority of the calnexin protein resides in the luminal portion of the ER, and is the membrane-bound paralog of the soluble ER protein Calreticulin. In mammalian cells, calnexin and calreticulin (CRT) are lectins that play key roles in glycoprotein folding within the ER, specifically binding oligosaccharide intermediates that contain a single terminal GlcManGlcNAc residue. Calnexin associates with newly synthesized, incompletely folded monomeric glycoproteins as well as numerous oligomeric protein complexes, including
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