LAUSR

Protein myristoylation, the addition of a 14-carbon saturated acyl group, is an abundant modification implicated in biological events as diverse as development, immunity, oncogenesis, and infections. N-myristoyltransferase (NMT) is the enzyme that catalyzes this modification. Many elegant studies have established the rules guiding the catalysis including substrate amino acid sequence requirement with the indispensable N-terminal glycine, and a co-translational mode of action. Recent advances in technology such as the development of fatty acid analogs, small molecule inhibitors, and new proteomic strategies, allowed a deeper insight into the NMT activity and function. Here we focus on discussing recent work demonstrating NMT as also a lysine myristoyltransferase, the enzyme's regulation by a previously unnoticed solvent channel, and mechanism of NMT regulation by protein-protein interactions. We also summarize recent findings of NMT's role in cancer, immunity and infections, and the advances in pharmacological targeting of myristoylation. Our analyses highlight opportunities for further understanding and discoveries.