Abstract
A long-standing enigma has been the role of N-linked glycans attached to many proteins in the endoplasmic reticulum (ER) and their co- and posttranslational remodelling along the secretory pathway. Evidence is accumulating that intracellular animal lectins play important roles in quality control and glycoprotein sorting along the secretory pathway. Calnexin and calreticulin in conjunction with associated chaperones promote correct folding and oligomerization of many glycoproteins in the ER. The discovery that one of these glycan modifications, mannose 6-phosphate, serves as a lysosomal targeting signal that is recognized by mannose 6-phosphate receptors has led to the notion that lectins may play more general roles in exocytotic protein trafficking (Chaps. 3–6). In present and subsequent chapters we discuss the role of intracellular lectins in quality control and their role in understanding the mechanisms underlying protein traffic in the secretory pathway (Chaps. 3–7) (Table 2.1).
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Gupta, G.S. (2012). Lectins in Quality Control: Calnexin and Calreticulin. In: Animal Lectins: Form, Function and Clinical Applications. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1065-2_2
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