N-Myristoyltransferase inhibition in HeLa

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.