Protein myristoylation in health and disease |
| |
Authors: | Megan H Wright William P Heal David J Mann Edward W Tate |
| |
Institution: | (1) Chemical Biology Centre, Imperial College London, Exhibition Rd., London, SW72AZ, UK;(2) Department of Chemistry, Imperial College London, Exhibition Rd., London, SW72AZ, UK;(3) Department of Life Sciences, Imperial College London, Exhibition Rd., London, SW72AZ, UK; |
| |
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. |
| |
Keywords: | Post-translational modification Drug design Myristoylation Lipidation Chemical proteomics |
本文献已被 SpringerLink 等数据库收录! |
|