Dataset Information

Co-translational and Post-translational protein myristoylation in HeLa cells

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. In E. Thinon, R. A. Serwa, et al., Nature Communications 2014, doi:10.1038/ncomms5919, 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Remigiusz Serwa

LAB HEAD: Edward W. Tate

PROVIDER: PXD002687 | Pride | 2018-07-31

REPOSITORIES: Pride

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

Thinon Emmanuelle E Serwa Remigiusz A RA Broncel Malgorzata M Brannigan James A JA Brassat Ute U Wright Megan H MH Heal William P WP Wilkinson Anthony J AJ Mann David J DJ Tate Edward W EW

Nature communications 20140926

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 prot ...[more]

PMID: 25255805

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			Action	DRS
	AzKTB.zip	Other
	AzRTB.zip	Other
	CoTMyrLFQ.zip	Other
	CoTMyrNMTI.zip	Other
	ET_A0.raw	Raw