Prenylation

From LipidomicsWiki

Protein prenylation
Prenylated proteins exert an important function in cellular regulation, particularly in cell proliferation, migration, vesicle trafficking, phagocytosis and apoptosis. In particular, the
small GTP-binding proteins act as dynamic bimodal relays in the transfer of intracellular signals, which are regulated by posttranslational lipid modification as outlined in chapter 4. With the exception of the Ran proteins, all Ras-related cyproteins studied so far are posttranslationally modified. While Arf proteins are myristoylated at the N-terminus, Ras, Rho/ Rac and Rab proteins contain in C-terminal cysteine-containing motif, which serves as attachment for one or two farnesyl or geranylgeranyl groups. The addition of farnesyl or geranylgeranyl moieties to the carboxyterminal cysteine residues is mediated by specific protein prenyltransferases. The enzymes that have been described to perform these
modifications, include the protein farneslytransferase (PFT), the protein geranylgeranyltransferase-I (PGGT-I), and the protein geranylgeranyltransferase-II (PGGT-II) or the Rab prenyltransferase.