Dataset Information

Identification of myristoylated proteins in Human cell lines (HEK293, HeLa, MCF7)

ABSTRACT: 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Edward W. Tate

PROVIDER: MSV000080690 | MassIVE | Tue Mar 28 19:32:00 BST 2017

SECONDARY ACCESSION(S): PXD001863

REPOSITORIES: MassIVE

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Publications

Multifunctional reagents for quantitative proteome-wide analysis of protein modification in human cells and dynamic profiling of protein lipidation during vertebrate development.

Broncel Malgorzata M Serwa Remigiusz A RA Ciepla Paulina P Krause Eberhard E Dallman Margaret J MJ Magee Anthony I AI Tate Edward W EW

Angewandte Chemie (International ed. in English) 20150325 20

Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direct detection of lipid-modified tryptic peptides by mass spectrometry. This method enables high-confidence identification of the myristoylated proteome on an unprecedented scale in cell culture, and allowed the first quantitative analysis of dynamic changes in protein lipidation during vertebrate embryonic development. ...[more]

PMID: 25807930

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