Proteins usually undergo modifications during or after their synthesis in the endoplasmic reticulum (ER) and Golgi apparatus network inside eukaryotic cells. One such modification is glycosylation, whereby sugars, such as glycans, are added to newly synthesized proteins. Glycans allow proteins to fold properly, in turn making them stable and biologically active for various cell processes. However, the exact mechanism of glycosylation in the ER and Golgi are still not known. One way to study the process of glycosylation during protein synthesis is to deliver synthetic proteins to specific cell organelles and observe their subcellular dynamics. But this is often hindered by the lack of specific delivery methods to organelles like the ER and Golgi.
