Modification-specific\nProteomic Analysis Reveals Cysteine\nS‑Palmitoylation Involved in Esophageal Cancer Cell Radiation

This study aimed to investigate the effects of radiation\n(RT) on\nprotein and protein S-palmitoylation levels in esophageal cancer (EC)\ncell lines. EC cells (<i>N</i> = 6) were randomly divided\ninto RT and negative control. The results revealed that 592 proteins\nwere identified in the RT group, including 326 upregulation proteins\nand 266 downregulation proteins. These differentially expressed proteins\nwere involved in cellular biological processes. S-palmitoylation sequencing\nanalysis revealed that 830 and 899 S-palmitoylation cysteine sites\nwere upregulated and downregulated, respectively. Differential S-palmitoylation\nproteins were primarily found in cellular processes, anatomical entities,\nand binding activities. Kyoto encyclopedia of genes and genomes (KEGG)\npathway and protein–protein interaction analysis revealed that\ndifferential S-palmitoylation proteins are involved in proteoglycans\nin cancer, shigellosis, EGFR tyrosine kinase inhibitor resistance,\nnucleocytoplasmic transport, and mineral absorption. In conclusion,\nthis study demonstrated that RT significantly affects protein expression\nand S-palmitoylation levels in EC cell lines, which has implications\nfor cancer biology-related cellular processes and pathways. These\nfindings enhance understanding of the molecular mechanisms underlying\nthe response of EC cells to RT treatment.