Co-translational glycosylation is a crucial post-translational modification process that plays a significant role in protein folding and secretion. This process involves the addition of oligosaccharide chains to nascent polypeptides as they are being synthesized by ribosomes. The glycosylation of proteins occurs in the endoplasmic reticulum (ER) and is essential for proper protein folding, stability, and trafficking within the cell.

Importance of Co-Translational Glycosylation

Co-translational glycosylation is a fundamental process that impacts the structure, function, and localization of proteins within the cell. The addition of glycans to nascent polypeptides during translation serves several essential functions:

  1. Protein Folding: Glycosylation aids in the proper folding of proteins by influencing their conformation and stability. The attachment of oligosaccharide chains can prevent misfolding and aggregation, thereby promoting the correct three-dimensional structure of the protein.
  2. Quality Control: Glycosylation acts as a quality control mechanism during protein synthesis. It helps to ensure that newly synthesized proteins attain their native conformation before being transported to their destination within the cell or secreted outside the cell.
  3. Protein Secretion: Co-translational glycosylation is closely linked to the secretory pathway. Proper glycosylation is necessary for efficient protein trafficking through the ER and Golgi apparatus, ultimately leading to their secretion from the cell.

Impact on Protein Folding

The addition of glycans during co-translational glycosylation has a profound impact on protein folding. The presence of oligosaccharide chains can influence the folding pathway and stability of nascent polypeptides. Several key mechanisms illustrate how co-translational glycosylation contributes to proper protein folding:

  1. Chaperone Function: Glycans can act as molecular chaperones, assisting in the correct folding of proteins by preventing non-productive interactions and promoting favorable folding pathways.
  2. Stabilization: Glycosylation can stabilize protein structures by shielding hydrophobic regions and reducing susceptibility to aggregation or misfolding.
  3. Influence on Disulfide Bond Formation: Co-translational glycosylation can impact disulfide bond formation, which is crucial for stabilizing protein structures.

Role in Protein Secretion

Co-translational glycosylation is intimately involved in the secretory pathway, where properly folded and modified proteins are transported from the ER to the Golgi apparatus and subsequently targeted for secretion. The following aspects highlight its role in protein secretion:

  1. ER-Associated Degradation (ERAD): Proper glycosylation serves as a signal for ER quality control mechanisms, ensuring that only correctly folded proteins are allowed to progress through the secretory pathway while misfolded proteins are targeted for degradation.
  2. Glycan Processing: Following co-translational glycosylation, further processing of glycans occurs in the ER and Golgi apparatus, leading to the generation of mature glycoproteins ready for secretion.
  3. Cell Surface Expression: Glycosylation influences cell surface expression of membrane proteins, impacting their stability and functionality at the plasma membrane.


In summary, co-translational glycosylation plays a critical role in protein folding and secretion within eukaryotic cells. By influencing protein folding, stability, and trafficking through the secretory pathway, this post-translational modification ensures that functional proteins are properly synthesized and targeted for secretion or cellular localization.

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