MassIVE MSV000096890

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Farnesylation in Th1 cells assessed by click chemistry

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Description

T helper cell activation is highly regulated to ensure proper immune responses while avoiding autoimmune reactions. Cell functions are determined by regulation of various levels of gene expression including posttranslational modifications of proteins. Protein prenylation is a posttranslational modification, where either a farnesyl- or a geranylgeranyl residue is added to a protein. It was shown to play a role in the differentiation and activation of various T cell populations, including Th1 cells. However, it is largely unknown which proteins are prenylated in Th1 cells and what the effect of farnesyl transferase inhibitor treatment, which blocks farnesylation of proteins, on protein prenylation is in this context. Here, using mass spectrometry, we show the identification of farnesylated proteins in human Th1 cells. This approach additionally uncovered the farnesylation of proteins, not yet known to be prenylated. These data provide valuable insights into novel aspects of protein prenylation in Th1 cell activation and deepen our understanding of the effects of farnesyl transferase inhibitor treatment on the human immune system. [doi:10.25345/C50C4SX3W] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Farnesylation ; Th1 cells ; Prenylation ; FTI ; Click Enrichment ; DatasetType:Proteomics

Contact

Principal Investigators:
(in alphabetical order) 		Katja Baerenfaller, Swiss Institute of Allergy and Asthma Research, Switzerland
Submitting User: JanaKoch

Publications

Koch J, Ruggia A, Beha C, Wipf I, Zhakparov D, Westermann P, Schmelzer S, Heider A, Fröhlich K, Baerenfaller K.
Uncovering protein prenylation in Th1 cells: novel prenylation sites and insights into statin and farnesyltransferase inhibition.
BMC Biol. 2025 Jul 31;23(1):233. Epub 2025 Jul 31.

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