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Global profiling of co- and post-translationally N-myristoylated proteomes in human cells.

Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW
Nat Commun 5 4919 (2014)
Related entries: 4c2x, 4c2z

Cited: 131 times
EuropePMC logo PMID: 25255805

Abstract

Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. Here, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined with potent and specific human N-myristoyltransferase (NMT) inhibition. Global quantification of N-myristoylation during normal growth or apoptosis allowed the identification of >100 N-myristoylated proteins, >95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for >70 substrates simultaneously across the proteome. Small-molecule inhibition through a conserved substrate-binding pocket is also demonstrated by solving the crystal structures of inhibitor-bound NMT1 and NMT2. The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.

Reviews - 4c2y mentioned but not cited (1)

  1. Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT). Salah Ud-Din AI, Tikhomirova A, Roujeinikova A. Int J Mol Sci 17 E1018 (2016)

Articles - 4c2y mentioned but not cited (5)

  1. Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW. Nat Commun 5 4919 (2014)
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