The synthesis of a polypeptide starts in the cytoplasm at the ribosomes,
then the genetic information from DNA is transcribed into mRNA in the cell nucleus. After that mRNA travels from the nucleus to the cytoplasm. Ribosomes in the cytoplasm read the mRNA and synthesize a polypeptide chain by linking together amino acids, this forms a primary structure of the polypeptide. Many polypeptides have a signal sequence, a specific sequence of amino acids, at the beginning. The signal sequence directs the ribosome-mRNA-polypeptide complex to the endoplasmic reticulum (ER). The ribosome docks on the ER, and the polypeptide continues its synthesis into the lumen of the ER. Inside the ER, the polypeptide undergoes various modifications, such as folding and addition of sugar groups (glycosylation). Proper folding and modifications are crucial for the polypeptide's function. Transport vesicles bud off from the ER carrying the modified polypeptide. These vesicles fuse with the Golgi apparatus, and the polypeptide is further processed as it moves through the Golgi stacks. The Golgi apparatus modifies and packages the polypeptide into vesicles. These vesicles can be secretory vesicles destined for the extracellular space. The vesicles move towards the cell membrane. Upon reaching the cell membrane, the vesicles undergo exocytosis, releasing their contents (the polypeptide) into the extracellular space. The polypeptide is now in the extracellular space outside the cell. Depending on the type of polypeptide, it may have specific functions such as being a signaling molecule, part of a structural protein, or an enzyme.