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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-12

AUTHORS

Emmanuelle Thinon, Remigiusz A. Serwa, Malgorzata Broncel, James A. Brannigan, Ute Brassat, Megan H. Wright, William P. Heal, Anthony J. Wilkinson, David J. Mann, Edward W. Tate

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. More... »

PAGES

4919

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncomms5919

    DOI

    http://dx.doi.org/10.1038/ncomms5919

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1038808525

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/25255805


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