Lipidiation

Lipidiation is a biochemical process involving the covalent attachment of lipid groups to a protein molecule. This post-translational modification plays a crucial role in the regulation of protein localization, stability, and function within the cell. Lipidiation can influence how proteins interact with cellular membranes, thereby affecting signal transduction, cellular trafficking, and membrane dynamics.

There are several types of lipidiation, including prenylation, myristoylation, palmitoylation, and glypiation. Prenylation involves the addition of farnesyl or geranylgeranyl groups to cysteine residues near the C-terminus of proteins, often targeting them to membranes. Myristoylation refers to the attachment of a myristoyl group, a 14-carbon saturated fatty acid, typically to an N-terminal glycine residue. Palmitoylation entails the reversible addition of palmitic acid (a 16-carbon saturated fatty acid) to cysteine residues, commonly modulating protein-membrane associations. Glypiation, also known as GPI-anchor attachment, involves linking proteins to the membrane via glycosylphosphatidylinositol (GPI) anchors.

Lipidiation is vital in numerous biological processes, including cell signaling, protein trafficking, and membrane organization. Misregulation of lipid modifications has been associated with various diseases, such as cancer, neurodegeneration, and infectious diseases, making lipidiation a significant target for therapeutic intervention.

Overall, lipidiation is a fundamental post-translational mechanism that governs protein functions by controlling their membrane association and localization within the cell.