Protein prenylation: Enzymes, therapeutics, and biotechnology applications

Charuta C. Palsuledesai, Mark D. Distefano

Research output: Contribution to journalReview articlepeer-review

142 Scopus citations


Protein prenylation is a ubiquitous covalent post-translational modification found in all eukaryotic cells, comprising attachment of either a farnesyl or a geranylgeranyl isoprenoid. It is essential for the proper cellular activity of numerous proteins, including Ras family GTPases and heterotrimeric G-proteins. Inhibition of prenylation has been extensively investigated to suppress the activity of oncogenic Ras proteins to achieve antitumor activity. Here, we review the biochemistry of the prenyltransferase enzymes and numerous isoprenoid analogs synthesized to investigate various aspects of prenylation and prenyltransferases. We also give an account of the current status of prenyltransferase inhibitors as potential therapeutics against several diseases including cancers, progeria, aging, parasitic diseases, and bacterial and viral infections. Finally, we discuss recent progress in utilizing protein prenylation for site-specific protein labeling for various biotechnology applications.

Original languageEnglish (US)
Pages (from-to)51-62
Number of pages12
JournalACS Chemical Biology
Issue number1
StatePublished - Jan 16 2015

Bibliographical note

Publisher Copyright:
© 2014 American Chemical Society.


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