Abstract
Lipid modification of proteins encompasses covalent linkage of three major classes of hydrophobic groups: fatty acids (myristate and/or palmitate), isoprenoids (farnesyl or geranylgeranyl) and glycosylphosphatidyl inositol (GPI) anchors. Attachment of each of these moieties regulates protein structure, intracellular localization, and function. Membrane interactions are essential for the function of many lipid modified proteins. The nature of the modifying group determines the strength, specificity and reversibility of membrane association. Given the involvement of lipid modified proteins in cancer and other disorders, drugs that inhibit lipid modification have the potential to be efficacious for treatment of human diseases.
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