The Golgi apparatus is a major collection and dispatch station of protein products received from the endoplasmic reticulum (ER). Proteins synthesized in the ER are packaged into vesicles, which then fuse with the Golgi apparatus. These cargo proteins are modified and destined for secretion via exocytosis or for use in the cell. The Golgi apparatus is also involved in lipid transport and lysosome formation.
Enzymatic reactions within the Golgi stacks occur exclusively near its membrane surfaces, where enzymes are anchored. This feature is in contrast to the ER, which has soluble proteins and enzymes in its lumen. Much of the enzymatic processing is a post-translational modification of proteins. For example, phosphorylation of oligosaccharides on lysosomal proteins occurs in the early CGN. Removal of mannose residues and addition of N-acetylglucosamine occur in medial cisternae. Addition of galactose and sialic acid occurs in the trans cisternae. Sulfation of tyrosines and carbohydrates occurs within the TGN. Other general post-translational modifications of proteins include the addition of carbohydrates (glycosylation) and phosphates (phosphorylation).
Protein modifications may form a signal sequence that determines the final destination of the protein. For example, the Golgi apparatus adds a mannose-6-phosphate label to proteins destined for lysosomes. Another important function of the Golgi apparatus is in the formation of proteoglycans. Enzymes in the Golgi append proteins to glycosaminoglycans, thus creating proteoglycans. Glycosaminoglycans are long unbranched polysaccharide molecules present in the extracellular matrix of animals.