{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15"],"submitter":["Schol M"],"pubmed_abstract":["Ceramides generated by the activity of the neutral sphingomyelinase 2 (nSMase2) play a pivotal role in stress responses in mammalian cells. Dysregulation of sphingolipid metabolism has been implicated in numerous inflammation-related pathologies. However, its influence on inflammatory cytokine-induced signaling is yet incompletely understood. Here, we used proximity labeling to explore the plasma membrane proximal protein network of nSMase2 and TNFα-induced changes thereof. We established Jurkat cells stably expressing nSMase2 C-terminally fused to the engineered ascorbate peroxidase 2 (APEX2). Removal of excess biotin phenol substantially improved streptavidin-based affinity purification of biotinylated proteins. Using our optimized protocol, we determined nSMase2-proximal biotinylated pr"],"journal":["Frontiers in immunology"],"pagination":["1435701"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11263205"],"repository":["biostudies-literature"],"pubmed_title":["Dynamic changes in the proximitome of neutral sphingomyelinase-2 (nSMase2) in TNFα stimulated Jurkat cells."],"pmcid":["PMC11263205"],"pubmed_authors":["Schol M","Hennig T","Wigger D","Schumacher F","Jansch L","Schempp R","Schneider-Schaulies S","Kleuser B","Stigloher C","Dolken L","van Ham M","Avota E"],"additional_accession":[]},"is_claimable":false,"name":"Dynamic changes in the proximitome of neutral sphingomyelinase-2 (nSMase2) in TNFα stimulated Jurkat cells.","description":"Ceramides generated by the activity of the neutral sphingomyelinase 2 (nSMase2) play a pivotal role in stress responses in mammalian cells. Dysregulation of sphingolipid metabolism has been implicated in numerous inflammation-related pathologies. However, its influence on inflammatory cytokine-induced signaling is yet incompletely understood. Here, we used proximity labeling to explore the plasma membrane proximal protein network of nSMase2 and TNFα-induced changes thereof. We established Jurkat cells stably expressing nSMase2 C-terminally fused to the engineered ascorbate peroxidase 2 (APEX2). Removal of excess biotin phenol substantially improved streptavidin-based affinity purification of biotinylated proteins. Using our optimized protocol, we determined nSMase2-proximal biotinylated pr","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-05-02T12:27:55.758Z","creation":"2025-06-01T01:16:41.479Z"},"accession":"S-EPMC11263205","cross_references":{"pubmed":["39044828"],"doi":["10.3389/fimmu.2024.1435701"]}}