What are N-linked and O-linked glycosylation of proteins?
Protein glycosylation is an important biochemical process in living organisms, involving the attachment of one or more sugar molecules to protein molecules. There are usually two types of glycosylation: N-linked glycosylation and O-linked glycosylation, which play significant roles in cell biology, pathobiology, and biochemical research.
1. N-linked glycosylation
N-linked glycosylation typically occurs as proteins enter the endoplasmic reticulum (ER), involving the initial construction of an oligosaccharide and its subsequent modification on the rough endoplasmic reticulum (RER). In this process, sugar molecules are attached to a specific asparagine nitrogen atom (usually the nitrogen atom in asparagine residues) in a polypeptide chain of the protein through a linkage called a glycan. Generally, the consensus sequence for N-linked glycosylation is Asn-X-Ser/Thr (X can be any amino acid except proline).
2. O-linked glycosylation
O-linked glycosylation typically occurs in the Golgi apparatus, involving the attachment of a monosaccharide molecule to the hydroxyl nitrogen atom of the protein, commonly on serine or threonine residues. Unlike N-linked glycosylation, O-linked glycosylation does not have a clear consensus sequence and begins with the attachment of a single sugar molecule, which may subsequently form complex sugar chains.
These two glycosylation processes not only play various physiological and biochemical roles in organisms (such as protein folding, stability, signal transduction, and transport) but also play important roles in the development of various diseases (such as cancer and metabolic diseases).
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