Biochemistry of protein prenylation.

Abstract

Covalent modification by isoprenoid lipids (prenylation) is now recognized as a mechanism to promote membrane interactions and biological activities of a variety of cellular proteins. Both the 15-carbon farnesyl and 20-carbon geranylgeranyl isoprenoids are involved in these modifications, which occur on carboxyl-terminal cysteine residues of proteins (Fig. 1). Known prenylated proteins include the nuclear protein lamin B and a number of GTP-binding regulatory proteins (G proteins) responsible for controlling a wide spectrum of signal transduction pathways. This review summarizes the development of, and recent studies in, the field of protein prenylation, with particular emphasis on the biochemistry of the processes involved. Several other recent reviews are available for more detailed coverage of aspects which receive limited attention here (1-3).