GluAs are N-glycosylated at several consensus sites within their extracellular domains [39]. The degree of complexity of this posttranslational modification, as reflected by differential resistance against glycosidase digestion, is often used as an indicator of protein maturation during transport along the secretory pathway. Here, we analyzed the effect of CNIH-2 co-expression on the glycosylation pattern of GluA2 instead of GluA1, as the extent of N-glycosylation of GluA2 was more prominent in HeLa cells than the one of GluA1.
