Glycoproteins calreticulin interaction

Calnexin and its soluble homologous calreticulin belong to the family of lectinlike chaperones. Their task is to interact with the partially trimmed monoglycosy-lated N-linked oligosaccharides and therefore contribute to an important part of the maturation and quality control mechanisms of glycoproteins [72]. The expression... 

Otteken, A., and Moss, B. (1996). Calreticulin interacts with newly synthesized human immunodeficiency virus Type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271, 97-103. 

Norgaard P, Westphal V, Tachibana C, Alsoe L, Holst B, Winther JR (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152 553 562 Oliver JD, Roderick HL, Llewellyn DH, High S (1999) ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10 2573-2582 Oliver JD, van der Wal FJ, Bulleid NJ, High S (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275 86-88... 

Glucosidase inhibitors, particularly castanospermine (CST), have proven to be useful tools to study the in vivo effects of blocking the interactions of calnexin and calreticulin with glycoproteins. Most studies support the view that these molecules function to promote the correct folding of glycoproteins. For example, treatment... 

Two models have been proposed to describe the interactions of calnexin and calreticulin with newly synthesized glycoproteins (Figure 2). In the first model [28, 32],... 

Sadasivan, B., Lehner, P.J., Ortmann, B., Spies, T., and Cresswell, P. Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP Immunity 1996 5, 103-114. 

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