N-Myristoyltransferase (NMT) covalently attaches a C14-fatty acid to the N-terminal glycine of proteins and has been proposed as a therapeutic target in cancer. We used quantitative proteomics to map protein expression changes for more than 2700 proteins in response to treatment with an NMT inhibitor in HeLa cells, and observed down-regulation of proteins involved in cell cycle regulation, and up-regulation of many proteins involved in the endoplasmic reticulum stress response. This study defines the cellular response to NMT inhibition at the proteome level, and provides a knowledgebase for targeting specific cancers with NMT inhibitors, potentially in combination with other targeted agents.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: HeLa ; Q-exactive ; N-myristoyltransferase inhibition ; spike-in SILAC
Principal Investigators: (in alphabetical order) |
Ed Tate, Department of Chemistry, Imperial College London, UK, N/A |
Submitting User: | ccms |
Thinon E, Morales-Sanfrutos J, Mann DJ, Tate EW.
N-Myristoyltransferase Inhibition Induces ER-Stress, Cell Cycle Arrest, and Apoptosis in Cancer Cells.
ACS Chem. Biol. 2016 Aug 19;11(8):2165-76. Epub 2016 Jun 7.
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