Dataset Information

Etomoxir as a Promiscuous Chemoproteomic Probe.

ABSTRACT: Primary hepatocytes from WT or Pex5KO mouse livers were treated with 100uM clickable etomoxir analogues and the proteins bound to etomoxir were pulled down and identified. The small molecule inhibitor etomoxir has been used for many years as a specific inhibitor of Cpt1 but these data show that etomoxir binds a large array of proteins and is not appropriate as a tool for evaluating the biological effects of fatty acid oxidation. Primary hepatocytes were treated with 100uM clickable etomoxir analogues and the proteins bound to etomoxir were pulled down and identified. The small molecule inhibitor etomoxir has been used for many years as a specific inhibitor of Cpt1 but these data show that etomoxir binds a large array of proteins and is not appropriate as a tool for evaluating the biological effects of fatty acid oxidation.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Primary Cell, Hepatocyte

SUBMITTER: Michael Wolfgang

LAB HEAD: Michael J. Wolfgang

PROVIDER: PXD045866 | Pride | 2024-10-17

REPOSITORIES: Pride

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			Action	DRS
	210826.xml	Xml
	210927_search.xml	Xml
	230704_search.xml	Xml
	LD-CS-LE_210826_WolfgangM_MW_BSA.raw	Raw
	LD-CS-LE_210826_WolfgangM_MW_BSA_20210910133544.raw	Raw

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Publications

Etomoxir repurposed as a promiscuous fatty acid mimetic chemoproteomic probe.

Choi Joseph J Smith Danielle M DM Lee Ye Jin YJ Cai Danfeng D Hossain Mohammad J MJ O'Connor Tamara J TJ Deme Pragney P Haughey Norman J NJ Scafidi Susanna S Riddle Ryan C RC Wolfgang Michael J MJ

iScience 20240802 9

Etomoxir has been used for decades as a popular small molecule inhibitor of carnitine palmitoyltransferase I, Cpt1, to block mitochondrial fatty acid β-oxidation. To test the specificity of etomoxir, we generated click chemistry-enabled reagents to label etomoxir binding proteins <i>in situ</i>. Etomoxir bound to Cpt1, but also bound to a large array of diverse proteins that metabolize and transport fatty acids in the cytoplasm, peroxisome, and mitochondria. Many of the most abundant proteins id ...[more]

PMID: 39252970

Dataset Information

Etomoxir as a Promiscuous Chemoproteomic Probe.

Dataset's files

Publications

Etomoxir repurposed as a promiscuous fatty acid mimetic chemoproteomic probe.

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