Which proteins are most likely to be glycosylated?

Glycosylation is a post-translational modification that typically occurs in the endoplasmic reticulum and Golgi apparatus, primarily on proteins that are destined for secretion or for incorporation into cellular membranes. Soluble and transmembrane proteins are the most likely to undergo glycosylation because this modification plays crucial roles in protein folding, stability, and cell signaling, and it assists in the protein's interactions with the extracellular environment or with other membrane-bound structures.

Transmembrane proteins, which span the lipid bilayer of the membrane, often have their extracellular domains glycosylated. This glycosylation can affect various functions, such as cell recognition and adhesion. Soluble proteins, which are secreted from the cell, also frequently receive glycosylation to aid in their stability and to help them function properly in biological processes.

In contrast, the other categories of proteins mentioned do not typically undergo glycosylation. Membrane-associated phospholipids do not undergo glycosylation because glycosylation is a modification that specifically targets proteins rather than lipids. Cytosolic enzymes are primarily located in the cytoplasm and do not enter the endoplasmic reticulum or Golgi apparatus, where glycosylation