Proteomics

Dataset Information

0

N-Myristoyltransferase inhibition in HeLa


ABSTRACT: 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Emmanuelle Thinon  

LAB HEAD: Ed Tate

PROVIDER: PXD003186 | Pride | 2016-06-13

REPOSITORIES: Pride

Dataset's files

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Publications

N-Myristoyltransferase Inhibition Induces ER-Stress, Cell Cycle Arrest, and Apoptosis in Cancer Cells.

Thinon Emmanuelle E   Morales-Sanfrutos Julia J   Mann David J DJ   Tate Edward W EW  

ACS chemical biology 20160607 8


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 have recently shown that selective NMT inhibition leads to dose-responsive loss of N-myristoylation on more than 100 protein targets in cells, and cytotoxicity in cancer cells. N-myristoylation lies upstream of multiple pro-proliferative and oncogenic pathways, but to date the complex substrate specificity of NMT has limited determina  ...[more]

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