Glycoproteins CNX-CRT interaction

From the long list of glycoproteins reported to associate with CNX/CRT, it may be concluded that most glycoproteins, irrespective of their final intracellular destination or soluble or membrane-bound status, transiently interact with CNX and CRT in mammalian cells (83-100). In all cases tested, addition of GI/GII inhibitors (such as castanospermine and 1-deoxynojirimycin or its /V-methyl or /V-butyl derivatives) prevented not only interaction of CNX/CRT with folding glycoproteins in mammalian cells but also dissociation of already formed glycoprotein-CNX/CRT complexes (55, 82-96, 101). Furthermore, no glycoprotein-CNX/CRT interaction was observed in GI- or Gll-dehcient cell lines (89, 102). As expected from differences observed in mammalian... 

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... 

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... 

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