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

Emmanuelle Thinon, Remigiusz A. Serwa, Malgorzata Broncel, James A. Brannigan, Ute Brassat, Megan H. Wright, William P. Heal, Anthony J. Wilkinson, David J. Mann and Edward W. Tate ()
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Emmanuelle Thinon: Imperial College London
Remigiusz A. Serwa: Imperial College London
Malgorzata Broncel: Imperial College London
James A. Brannigan: York Structural Biology Laboratory, University of York
Ute Brassat: Imperial College London
Megan H. Wright: Imperial College London
William P. Heal: Imperial College London
Anthony J. Wilkinson: York Structural Biology Laboratory, University of York
David J. Mann: Imperial College London
Edward W. Tate: Imperial College London

Nature Communications, 2014, vol. 5, issue 1, 1-13

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms5919

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