Intracellular lectins involved in folding and transport in the endoplasmic reticulum

Abstract

Glycosylation is a highly sophisticated post-translational modification of proteins that occurs in the endoplasmic reticulum (ER) and the Golgi apparatus. The vital biological functions served by protein glycosylation can be separated into two types. The first is the role of glycosylation in the extracellular environment, where a variety of sugar chains participate in protein secretion and stability, cell-cell adhesion and signaling, innate immunity, embryogenesis, and morphogenesis. Another role is in quality control of glycoproteins in the ER, a topic that has received recent attention. Quality control of glycoproteins is categorized into three kinds of reactions; the first is folding of newly synthesized glycoproteins, the second is ER-associated degradation of terminally misfolded or unassembled glycoproteins, and the last is sorting and transport of glycoproteins between organelles. In all three processes, N-glycans on the glycoproteins are used as tags to initiate the reactions. The process of glycosylation is conserved in yeast, plants, invertebrates and vertebrates, including mammals. Here, I focus on the intracellular lectins that participate in these processes and discuss the role of glycosylation based on the structural differences of N-glycans.