myristoylaation

Myristoylation is a type of lipid modification where myristic acid, a saturated fatty acid with a 14-carbon chain, is covalently attached to a protein. This process typically occurs at the N-terminus of a protein, specifically on the alpha-amino group of an N-terminal glycine residue. The attachment is mediated by an enzyme called N-myristoyltransferase (NMT). Myristoylation is considered a permanent modification because the myristoyl group is generally not removed from the protein once attached.

The primary function of myristoylation is to anchor proteins to cellular membranes, particularly the inner leaflet of the plasma membrane. This membrane association can be crucial for protein localization, stability, and interaction with other cellular components. Myristoylated proteins can be involved in a wide range of cellular processes, including signal transduction, protein trafficking, and viral assembly. The hydrophobic nature of the myristoyl chain allows it to insert into the lipid bilayer, effectively tethering the protein to the membrane. In some cases, myristoylation can also influence protein conformation and activity. The specificity of NMT for N-terminal glycine residues suggests a recognition mechanism that ensures the correct proteins are modified.