Protein Prenylation


Protein prenylation ranks among the most common lipid modifications of proteins, affecting up to 2% of the proteins in the mammalian proteome.
It involves the formation of a thioether linkage between a 15-carbon or 20-carbon isoprenoid moiety and one or two cysteine residues near the C-terminus of the target protein. Farnesylated and geranylgeranylated proteins include members of the Ras, Rho, Rac, Rap and Rab families, the γ subunit of heterotrimeric G proteins, centromeric proteins and many more.
The prenyl moiety is essential for the reversible association of the target protein with the intracellular membrane and modulates protein-protein interactions.
Jena Bioscience’s innovative protein prenylation products provide the basis for next generation prenylome studies with important implications for human health and disease.

Protein Prenyl Transferases

Protein prenyltransferases (FTase, GGTase-I and RabGGTase) and engineered mutants for in vitro prenylation assays

Lipid Donors

Natural and modified lipid donors that allow to detect femtomolar amounts of prenylatable proteins

FTase Substrates and Related Proteins

Suitable substrates for protein farnesyltransferase and corresponding mutants

GGTase-I Substrates and Related Proteins

Suitable substrates for protein geranylgeranyltransferase type I and corresponding deletion mutants with truncated C-terminus

RabGGTase Substrates and Related Proteins

Suitable substrates for protein geranylgeranyltransferase type II (RabGGTase) and corresponding mutants

Inhibitors

Potential and selective inhibitors for the different protein prenyltransferases

Selected References

Hougland et al. (2009) Getting a handle on protein prenylation. Nat. Chem. Biol. 5 (4):197
Nguyen et al. (2009) Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat. Chem. Biol. 5 (4):227
Konstantinopoulos et al. (2007) Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets. Nat. Rev. Drug Discov. 6 (7):541
McTaggart et al. (2006) Isoprenylated proteins. Cell. Mol. Life Sci. 63:255