Farnesoylated

Farnesoylated refers to the post-translational modification of a protein by the addition of a farnesyl group. Farnesyl is a 15-carbon isoprenoid lipid. This process, known as farnesylation, is a type of prenylation, which is the covalent attachment of lipid moieties to proteins. Farnesylation is catalyzed by enzymes called farnesyltransferases, which transfer the farnesyl group from farnesyl pyrophosphate to a cysteine residue at the C-terminus of a target protein. This modification typically occurs on proteins that have a C-terminal CAAX motif, where C is cysteine, A is any aliphatic amino acid, and X is any amino acid.

The farnesyl group is hydrophobic, and its addition to a protein increases the protein's lipophilicity. This increased lipophilicity can facilitate the protein's association with cell membranes, influencing its localization and function. Farnesylation plays a crucial role in the signaling pathways of various cellular processes, including cell growth, differentiation, and survival. Many proteins involved in signal transduction, such as Ras proteins and certain nuclear lamins, are farnesoylated. Aberrant farnesylation is implicated in various diseases, including cancer, making farnesyltransferase inhibitors a subject of therapeutic interest. The study of farnesoylated proteins is important for understanding cellular biology and developing treatments for related diseases.