Post-translational isoprenylation refers to the chemical modification of a protein following its synthesis, specifically the attachment of an isoprenyl group to certain amino acids within the protein structure. Isoprenylation commonly involves the addition of a lipophilic (hydrophobic) molecule derived from isoprene units, such as farnesyl or geranylgeranyl, to specific cysteine residues.
Isoprenylation plays a crucial role in modifying the function, localization, and interactions of various proteins, particularly those involved in cellular signaling and membrane binding. It serves as a lipid anchor that facilitates the attachment of the modified protein to cellular membranes, thereby enabling its proper positioning and interaction with other membrane-bound proteins and lipid components.
This post-translational modification is involved in a wide range of biological processes, including signal transduction, intracellular trafficking, cell cycle regulation, and protein-protein interactions. Isoprenylation is essential for the proper functioning of critical signaling proteins, such as Ras and Rho GTPases, whose membrane association and subsequent activation depend on the covalent attachment of an isoprenyl group.
Aberrations in post-translational isoprenylation have been associated with various human diseases, including cancer, neurological disorders, and cardiovascular conditions. Therefore, understanding the mechanisms and functional consequences of isoprenylation is of great importance in both basic research and the development of therapeutic interventions.
