Calreticulin Are Lectins Specific for Monoglucosylated Oligosaccharides

Calnexin and Calreticulin Are Lectins Specific for Monoglucosylated Oligosaccharides 

The selective association of CNX/CRT with incompletely assembled glycoproteins and the close correlation of such interactions with their residence in the ER indicated that the lectins participated in the retention of incompletely folded glycoproteins (117). Together with the selective reglucosylation of incompletely folded glycoproteins, these 

Folding facilitation and ER retention of misfolded species mediated by glycoprotein-CNX/CRT interaction are not required for cell viability under normal growth conditions. Mammalian and yeast cells deficient in GI or GII activities, in which monoglucosylated glycans cannot be 

GI/GII inhibitors prevented VSV maturation by interfering with G protein folding, as well as formation of infectious human immunodeficiency virus (HIV) type I particles, probably due to misfolding of loop V1-V2 in gpl20 (141, 147, 148). In addition, glucosidase inhibitors 

Some misfolded proteins are not retrotranslocated to the cytosol for proteasomal degradation. In S. cerevisiae, some incompletely folded proteins escaped the ER and, after reaching the Golgi, were routed to the vacuole for degradation. Genetic evidence indicated that targeting to the 

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