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Protein myristoylation in health and disease

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Journal of Chemical Biology

Abstract

N-myristoylation is the attachment of a 14-carbon fatty acid, myristate, onto the N-terminal glycine residue of target proteins, catalysed by N-myristoyltransferase (NMT), a ubiquitous and essential enzyme in eukaryotes. Many of the target proteins of NMT are crucial components of signalling pathways, and myristoylation typically promotes membrane binding that is essential for proper protein localisation or biological function. NMT is a validated therapeutic target in opportunistic infections of humans by fungi or parasitic protozoa. Additionally, NMT is implicated in carcinogenesis, particularly colon cancer, where there is evidence for its upregulation in the early stages of tumour formation. However, the study of myristoylation in all organisms has until recently been hindered by a lack of techniques for detection and identification of myristoylated proteins. Here we introduce the chemistry and biology of N-myristoylation and NMT, and discuss new developments in chemical proteomic technologies that are meeting the challenge of studying this important co-translational modification in living systems.

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Acknowledgments

MHW thanks the Chemical Biology Centre, Imperial College London, for the award of a studentship. WPH is supported by a Research Project Grant from Cancer Research UK to EWT and DJM (grant C29637/A9913). EWT thanks the Biotechnology and Biological Sciences Research Council (BBSRC), UK, for the award of a David Phillips Research Fellowship (grant BB/D02014X/1).

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Correspondence to Edward W. Tate.

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Wright, M.H., Heal, W.P., Mann, D.J. et al. Protein myristoylation in health and disease. J Chem Biol 3, 19–35 (2010). https://doi.org/10.1007/s12154-009-0032-8

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