Proteomic data _ identification of neutral sphingomyelinase-2 (nsm2) proximal proteins by apex2-mediated proximity labeling in jurkat cells

Other: Proteomic mass spectrometry data supplementing the data published in the thesis: Identification of NSM2 proximal proteins by APEX2-mediated proximity labeling in Jurkat cells. TechnicalInfo: The csv files contain tables that list proteins identified by label free LC-MS and their Log2 Fold Changes (Log2FC) and p values. Information about the individual csv files can be found in the "readme.txt”. Abstract: A proximity labeling strategy was used based on the engineered ascorbate peroxidase 2 (APEX2) to explore the neutral sphingomyelinase 2 (NSM2) proximitome, specifically in Jurkat cells. For this purpose, cell lines stably expressing NSM2 fused to APEX2 at the C-terminus were generated. NSM2-APEX2 proximal proteins covalently labeled with biotin were purified using streptavidin-coated beads and identified by mass spectrometry (MS). The first analysis of NSM2-APEX2 labeling by MS accurately identified proteins under steady-state conditions (published in 10.3390/ijms25063247). Further, I applied the proximity labeling protocol to elucidate TNFα-induced alterations in the NSM2 proximitome within the first 5 minutes of stimulation (published in 10.3389/fimmu.2024.1435701). The NSM2 proximal network and its TNFα-induced changes provide a valuable resource for further investigations into the involvement of NSM2 in the early signaling pathways triggered by TNFα.