Final answer:
N-glycosylated proteins are primarily destined to be secreted from the cell or incorporated into the plasma membrane following modifications in the RER and Golgi apparatus.
Step-by-step explanation:
Proteins that undergo N-glycosylation in the rough endoplasmic reticulum (RER) are often destined for secretion or incorporation into the plasma membrane. N-glycosylation is a modification that occurs as proteins pass through the pathway of the endomembrane system. After synthesis and initial glycosylation in the RER, these proteins are transported to the Golgi apparatus. Here, they undergo final modifications, including the completion of the glycosylation process. Once the process is finalized, the glycoproteins are packaged into secretory vesicles that bud from the trans face of the Golgi apparatus. These vesicles ultimately fuse with the plasma membrane, which either incorporates the glycoproteins as membrane components or secretes them outside the cell, contributing to the cell's interaction with its environment. Therefore, proteins that are N-glycosylated are typically expected to perform functions related to the cell's extracellular matrix or communication with other cells rather than being retained in the endoplasmic reticulum, imported into a cell via endocytosis, or serving as peroxisome enzymes.
The final answer, in two line explanation in 300 words: N-glycosylated proteins are most commonly processed through the endomembrane system to be either secreted from the cell or integrated into the plasma membrane, reflecting their roles in cell-to-cell interactions and the composition of the extracellular matrix. This pathway of modifications and travel through the endomembrane system indicates that they are not typically retained long-term in the endoplasmic reticulum, imported by endocytosis, or associated with peroxisomes.