期刊
NATURE COMMUNICATIONS
卷 5, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms5919
关键词
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资金
- Cancer Research UK [C29637/A10711, C29637/A9913]
- Biotechnology and Biological Sciences Research Council [BB/D02014X/1]
- Engineering and Physical Sciences Research Council
- European Union (Marie Curie Intra European Fellowships) [PIEF-GA-2010-273868, PIEF-GA-2011-299740]
- Medical Research Council [0900278]
- Biotechnology and Biological Sciences Research Council [BB/D02014X/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/K039946/1] Funding Source: researchfish
- Medical Research Council [G0900278] Funding Source: researchfish
- BBSRC [BB/D02014X/1] Funding Source: UKRI
- EPSRC [EP/K039946/1] Funding Source: UKRI
- MRC [G0900278] Funding Source: UKRI
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 4100 N-myristoylated proteins, 495% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for 470 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.
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