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ABSTRACT: Background
T helper 1 (Th1) cell activation is an essential process for immune responses and is tightly regulated, including the prenylation of proteins critical for T cell function. Prenylation facilitates membrane association and protein function and, according to current consensus, is confined to C-terminal prenylation motifs. However, the full extent of the prenylated proteome, a broader understanding of prenylation sites, and the effects of inhibiting prenylation or blocking isoprenoid synthesis using statins remain incompletely understood. To address these gaps, we aimed to comprehensively identify and characterise protein prenylation in Th1 cells.Results
Using a click chemistry-based enrichment approach followed by mass spectrometry in primary in vitro-differentiated
SUBMITTER: Koch J
PROVIDER: S-EPMC12315405 | biostudies-literature | 2025 Jul
REPOSITORIES: biostudies-literature