Role of Proteases in the Regulation of N-Myristoyltransferase

N-Myristoyltransferase (NMT) catalyzes the amide-linked addition of the myristoyl (C14:0) moiety to the amino-terminal glycine of substrate molecules. The upregulation of NMT in cancerous states was originally reported by our group, and subsequently this protein has drawn significant interest as a therapeutic target. However, the regulation of this enzyme in various physiological states is still in a state of infancy. NMT possesses PEST sequences and is a target for m-calpain-mediated degradation. The two isoforms, NMT1 and NMT2, interact differentially with the proteases caspase-3 and m-calpain. Recently, we have shown that the interaction of these isoforms (i.e., NMT1 and NMT2) with caspases regulates co- and posttranslational protein myristoylation. In this chapter, we have discussed the findings of the regulation of NMT functions by various proteases and the effects of proteolytic processing of NMT on its biochemical behavior.