Recent searches
Search options
RT @biorxivpreprint: Multifaceted proteome analysis at solubility, redox, and expression dimensions for target identification https://www.biorxiv.org/cgi/content/short/2023.08.31.555796v1 #bioRxiv https://www.biorxiv.org/cgi/content/short/2023.08.31.555796v1
bioRxivMultifaceted proteome analysis at solubility, redox, and expression dimensions for target identificationMultifaceted interrogation of the proteome deepens the system-wide understanding of biological systems; however, mapping the redox changes in the proteome has so far been significantly more challenging than expression and solubility/stability analyses. Here, we devise the first high-throughput redox proteomics approach integrated with expression analysis (REX) and combine it with Proteome Integral Solubility Alteration (PISA) assay. The whole PISA-REX experiment with up to four biological replicates can be multiplexed into a single tandem mass tag TMTpro set. For benchmarking this compact tool, we analyzed HCT116 cells treated with auranofin, showing great improvement compared with previous such studies. Then we applied PISA-REX to study proteome remodeling upon stimulation of human monocytes by interferon α. We also studied the proteome changes in plasmacytoid dendritic cells isolated from wild type vs. Ncf1-mutant mice treated with interferon α, showing that NCF1 deficiency enhances the STAT1 pathway and modulates the expression, solubility and redox state of interferon-induced proteins. Providing comprehensive multifaceted information on the proteome, the compact PISA-REX has the potential to become an industry standard in proteomics and to open new windows into the biology of health and disease.
### Competing Interest Statement
The authors have declared no competing interest.