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Functional proteomics-based investigation of the cellular response to farnesyl transferase inhibition in lung cancer (farnesylated proteins pull-down)

ABSTRACT: The subcellular localization of proteins can be highly dynamic and regulated by post-translational modifications. Farnesylation is a lipid modification that enables anchoring of proteins to cellular membranes, and thus, spatially resolved signaling and activity. Due to the importance of farnesylation for cellular functions, farnesyltransferase inhibitors (FTIs) including tipifarnib were developed and are being tested in oncology clinical trials. The current lack of knowledge on the functional impact of FTIs on hundreds of farnesylation substrates limits response prediction and their use in cancer precision medicine. Here, we report a global functional proteomics investigation of farnesylation and the impact of tipifarnib in multiple lung cancer cell lines. This dataset covers metabolic labelling-based identification of farnesylated proteins using mass spectrometry.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

DISEASE(S): Lung Cancer

SUBMITTER: Georgios Mermelekas

LAB HEAD: Lukas Orre

PROVIDER: PXD050725 | Pride | 2025-04-09

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	FTI_MS_rawfile_list_v240307.xlsx	Xlsx
	FarnesylatedProtein_PullDown_H1568_genes_table.txt	Txt
	FarnesylatedProtein_PullDown_H1975_genes_table.txt	Txt
	FarnesylatedProtein_PullDown_H2009_genes_table.txt	Txt
	FarnesylatedProtein_PullDown_H727_genes_table.txt	Txt

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Functional proteomics-based investigation of the cellular response to farnesyl transferase inhibition in lung cancer (subcellular localization and relocalization analysis)

Project description:The subcellular localization of proteins can be highly dynamic and regulated by post-translational modifications. Farnesylation is a lipid modification that enables anchoring of proteins to cellular membranes, and thus, spatially resolved signaling and activity. Due to the importance of farnesylation for cellular functions, farnesyltransferase inhibitors (FTIs) including tipifarnib were developed and are being tested in oncology clinical trials. The current lack of knowledge on the functional impact of FTIs on hundreds of farnesylation substrates limits response prediction and their use in cancer precision medicine. Here, we report a global functional proteomics investigation of farnesylation and the impact of tipifarnib in multiple lung cancer cell lines. This dataset includes global mapping of protein localization using our SubCellBarCode method, and analyses of tipifarnib-dependent protein relocalization.

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Project description:The subcellular localization of proteins can be highly dynamic and regulated by post-translational modifications. Farnesylation is a lipid modification that enables anchoring of proteins to cellular membranes, and thus, spatially resolved signaling and activity. Due to the importance of farnesylation for cellular functions, farnesyltransferase inhibitors (FTIs) including tipifarnib were developed and are being tested in oncology clinical trials. The current lack of knowledge on the functional impact of FTIs on hundreds of farnesylation substrates limits response prediction and their use in cancer precision medicine. Here, we report a global functional proteomics investigation of the impact of tipifarnib in multiple lung cancer cell lines. This dataset includes proteome-wide analysis of the effects of tipifarnib at 6, 12, 24, 48 h timepoints. The data covers experiments in five lung cancer cell lines (NCI-H727, NCI-H1568, NCI-H1975, NCI-H2009 and NCI-H1944).

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