Farnesyylaatio

Farnesyylaatio is a post-translational modification (PTM) of proteins in which a farnesyl group is covalently attached to a protein. This modification is also known as protein farnesylation. The farnesyl group is a 15-carbon isoprenoid lipid molecule that is derived from the mevalonate pathway, which is responsible for cholesterol biosynthesis.

In farnesylation, the enzyme farnesyltransferase (FTase) catalyzes the transfer of the farnesyl group from its donor molecule, farnesyl pyrophosphate (FPP), to the target protein. This modification typically occurs at the carboxyl terminus of the protein, where the farnesyl group is attached via a thioether bond. Farnesylation is an essential step in the biological activity of many proteins, and it is involved in various cellular processes, including signal transduction, protein-protein interactions, and cell cycle regulation.

Abnormal levels of farnesylated proteins have been implicated in various diseases, including cancer, where they contribute to oncogenesis and tumor progression. Inhibitors of farnesyltransferase have been developed as therapeutic agents to target these diseases.

Farnesylation is also involved in the pathogenesis of certain neurodegenerative diseases, such as Parkinson's disease, where farnesylated proteins play a role in the regulation of mitochondrial function and cell survival.

Studies on farnesylation have also provided insights into the biosynthesis of cholesterol and other isoprenoid compounds. A better understanding of the mechanisms of farnesylation and its role in various diseases may lead to the development of new therapeutic strategies and the identification of new targets for disease treatment.