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Isoprenylation/methylation is an important posttranslational lipid modification: the covalent addition of a 15 carbon farnesyl or a 20-carbon geranylgeranyl group to the C-terminus of a protein results in a substantial increase in hydrophobicity. All known G proteins are modified in this way, making the pathway of central interest for an understanding of signal transduction. From nematode to human, many eukaryotic proteins are reported to be isoprenylated. Known prenylated prtoteins include fungal mating factors, nuclear lamins, Ras and Ras-related GTP-binding proteins (G proteins), and the subunits of trimeric G proteins, protein kinases and at least one viral prtoein. Prenylation promotes membrane interactions of most of these proteins, which is not surprising given the hydrophobicity of the lipids involved. In addition, prenylation appears to play a major role in several protein-protein interaction.
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