{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schneider H"],"funding":["European Research Council","NIAID NIH HHS"],"pagination":["2281-2295"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6705488"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["476(16)"],"pubmed_abstract":["Transmembrane mucin MUC17 is an integral part of the glycocalyx as it covers the brush border membrane of small intestinal enterocytes and presents an extended <i>O</i>-glycosylated mucin domain to the intestinal lumen. Here, we identified two unknown phosphorylated serine residues, S4428 and S4492, in the cytoplasmic tail of human MUC17. We have previously demonstrated that MUC17 is anchored to the apical membrane domain via an interaction with the scaffolding protein PDZK1. S4492, localized in the C-terminal PDZ binding motif of MUC17, was mutated to generate phosphomimetic and phosphodeficient variants of MUC17. Using Caco-2 cells as a model system, we found that induction of an inflammatory state by long-term stimulation with the proinflammatory cytokine TNFα resulted in an increase of"],"journal":["The Biochemical journal"],"pubmed_title":["The human transmembrane mucin MUC17 responds to TNFα by increased presentation at the plasma membrane."],"pmcid":["PMC6705488"],"funding_grant_id":["U01 AI095473","694181"],"pubmed_authors":["Pelaseyed T","Schneider H","Dolan B","Martinez-Abad B","Hansson GC","Arike L","Berger E"],"additional_accession":[]},"is_claimable":false,"name":"The human transmembrane mucin MUC17 responds to TNFα by increased presentation at the plasma membrane.","description":"Transmembrane mucin MUC17 is an integral part of the glycocalyx as it covers the brush border membrane of small intestinal enterocytes and presents an extended <i>O</i>-glycosylated mucin domain to the intestinal lumen. Here, we identified two unknown phosphorylated serine residues, S4428 and S4492, in the cytoplasmic tail of human MUC17. We have previously demonstrated that MUC17 is anchored to the apical membrane domain via an interaction with the scaffolding protein PDZK1. S4492, localized in the C-terminal PDZ binding motif of MUC17, was mutated to generate phosphomimetic and phosphodeficient variants of MUC17. Using Caco-2 cells as a model system, we found that induction of an inflammatory state by long-term stimulation with the proinflammatory cytokine TNFα resulted in an increase of","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Aug","modification":"2025-04-22T20:25:16.845Z","creation":"2020-10-01T07:14:42Z"},"accession":"S-EPMC6705488","cross_references":{"pubmed":["31387973"],"doi":["10.1042/BCJ20190180"]}}