Recent advances in the study of prenylated proteins.
Post-translational modification of proteins with isoprenoids was first recognized as a general phenomenon in 1984. In recent years, our understanding, including mechanistic studies, of the enzymatic reactions associated with these modifications and their physiological functions has increased dramatically. Of particular functional interest is the role of prenylation in facilitating protein-protein interactions and membrane-associated protein trafficking. The loss of proper localization of Ras proteins when their farnesylation is inhibited has also permitted a new target for anti-malignancy pharmaceuticals. Recent advances in the enzymology and function of protein prenylation are reviewed in this article.
Sinensky
M
M
Department of Biochemistry and Molecular Biology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, TN 37614-0581, USA. sinensky@etsu.edu
D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors; D000595:Amino Acid Sequence; D000970:Antineoplastic Agents / Q000737:chemistry; D015195:Drug Design; D051231:Farnesyltranstransferase; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D017368:Protein Prenylation; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae; D018631:ras Proteins / Q000378:metabolism
D000970:Antineoplastic Agents; D008565:Membrane Proteins; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase; D018631:ras Proteins