Multi-functional capture reagents reported here enable robust identification of metabolically-tagged myristoylated proteomes with unprecedented confidence resulting from the combination of chemical probe-based enrichment, and release and direct detection of lipid-modified peptides by MS. Whilst capture reagents containing enzymatically cleavable linkers have been previously reported they typically require an extra proteolytic step and their capacity to enable detection of lipidated peptides has not been demonstrated. Herein, we report the largest database (85 counts) of experimentally validated human proteins that are myristoylated at an endogenous level in living cells. Furthermore, we demonstrate the first profile of myristoylation in a living multicellular organism and the confident identification of over 50 novel targets. Importantly, this is also the first example of analysis of any protein lipidation event during development. Our methodology is novel in analytical/chemical approach, and provides quantitative and dynamic information. This submission concerns myristoylated proteomes of human origin.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Human ; Protein myristoylation ; Myristoylated peptides ; chemical probes ; LC-MS/MS
Principal Investigators: (in alphabetical order) |
Edward W. Tate, Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK, N/A |
Submitting User: | ccms |
Broncel M, Serwa RA, Ciepla P, Krause E, Dallman MJ, Magee AI, Tate EW.
Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.
Angew. Chem. Int. Ed. Engl. 2015 May 11;54(20):5948-51. Epub 2015 Mar 25.
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