Abstract
Over the last 12 years or so, a group of posttranslational modifications of proteins with various lipid molecules has been identified in eukaryotic cells (for reviews see Schmidt 1989; McIlhinney 1990; Gordon et al. 1991; Magee 1991). In many cases these modifications have been shown to be essential for the subcellular localization of the proteins carrying them. Many intracellular proteins are now known to carry fatty acid modifications which serve such a purpose. The 14 carbon saturated fatty acid myris-tate (C14:0) is amide-linked to the NH2-terminal of a range of proteins, exemplified by the pp60src proto-oncogene product. Site-directed mutagenesis has been used to demonstrate that this acylation is required both for membrane localization and transforming activity. The myristoylation enzyme has been isolated and is highly specific for acyl chain length. Inhibitors which interfere with this pathway provide an attractive approach to specific chemotherapies of cancers and viral infections including HIV.
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© 1997 Springer-Verlag Berlin Heidelberg
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Giannakouros, T.G. (1997). Lipid Modifications of Proteins. In: Kamp, R.M., Choli-Papadopoulou, T., Wittmann-Liebold, B. (eds) Protein Structure Analysis. Springer Lab Manual. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-59219-5_18
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DOI: https://doi.org/10.1007/978-3-642-59219-5_18
Publisher Name: Springer, Berlin, Heidelberg
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