Prenylation or isoprenylation is the addition of hydrophobic molecules to a protein to facilitate its attachment to the cell membrane. The result is similar to that of all lipid anchored proteins (e.g. the GPI anchor). All isoprenylation chains are products of the HMG-CoA reductase pathway: geranylgeraniol (GG), farnesol and dolichol.
Proteins that undergo prenylation include ras, which plays a central role in the development of cancer. This suggests that inhibitors of prenylation enzymes (e.g. farnesyltransferase) may influence tumor growth.
Prenylation or isoprenylation or lipidation is the addition of hydrophobic molecules to a protein.
It is usually assumed that prenyl groups facilitate attachment to cell membranes, similar to lipid anchor like the GPI anchor, though direct evidence is missing.
Prenyl groups have been shown to be important for protein-protein binding through specialized prenyl-binding domains.
These "prenyl" groups are made from the chemical species isoprene, a fundamental and ubiquitous chemical building block in plants and animals.
Prenyl groups seem to play a role in anchoring proteins to cell membranes, among other functions.
After Glomset, Gelb, and colleagues had demonstrated the structure of these prenyl groups, researchers elsewhere found that a certain type of protein responsible for cellular switching and growth functions, called the "ras" protein, has a farnesyl group attached to it which is critical to the function of the protein.
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