{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ehrencrona E"],"funding":["Sahlgrenska Academy","European Research Council","Swedish Cancer Foundation","IngaBritt and Arne Lundberg Foundation","NIAID NIH HHS","Knut and Alice Wallenberg Foundation","Sahlgrenska universitetssjukhuset","Swedish Cancer Society","National Institutes of Health","Swedish Research Council","NIAID"],"pagination":["100871"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8267560"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["297(1)"],"pubmed_abstract":["Mucus forms an important protective barrier that minimizes bacterial contact with the colonic epithelium. Intestinal mucus is organized in a complex network with several specific proteins, including the mucin-2 (MUC2) and the abundant IgGFc-binding protein, FCGBP. FCGBP is expressed in all intestinal goblet cells and is secreted into the mucus. It is comprised of repeated von Willebrand D (vWD) domain assemblies, most of which have a GDPH amino acid sequence that can be autocatalytically cleaved, as previously observed in the mucins MUC2 and mucin-5AC. However, the functions of FCGBP in the mucus are not understood. We show that all vWD domains of FCGBP with a GDPH sequence are cleaved and that these cleavages occur early during biosynthesis in the endoplasmic reticulum. All cleaved fragme"],"journal":["The Journal of biological chemistry"],"pubmed_title":["The IgGFc-binding protein FCGBP is secreted with all GDPH sequences cleaved but maintained by interfragment disulfide bonds."],"pmcid":["PMC8267560"],"funding_grant_id":["2017/360","2019-01134","U01AI095473","U01 AI095473","2018-0117","ALFGBG-440741","2017-00958","2015-03047","694181","CAN2016/487","2015-070","2017-0028","ALFGBG-724681"],"pubmed_authors":["Ehrencrona E","van der Post S","Trillo-Muyo S","Rodriguez-Pineiro AM","Backstrom M","Recktenwald CV","Hansson GC","Gallego P","Johansson MEV","Garcia-Bonete MJ"],"additional_accession":[]},"is_claimable":false,"name":"The IgGFc-binding protein FCGBP is secreted with all GDPH sequences cleaved but maintained by interfragment disulfide bonds.","description":"Mucus forms an important protective barrier that minimizes bacterial contact with the colonic epithelium. Intestinal mucus is organized in a complex network with several specific proteins, including the mucin-2 (MUC2) and the abundant IgGFc-binding protein, FCGBP. FCGBP is expressed in all intestinal goblet cells and is secreted into the mucus. It is comprised of repeated von Willebrand D (vWD) domain assemblies, most of which have a GDPH amino acid sequence that can be autocatalytically cleaved, as previously observed in the mucins MUC2 and mucin-5AC. However, the functions of FCGBP in the mucus are not understood. We show that all vWD domains of FCGBP with a GDPH sequence are cleaved and that these cleavages occur early during biosynthesis in the endoplasmic reticulum. All cleaved fragme","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jul","modification":"2026-05-09T07:40:42.072Z","creation":"2022-02-10T21:49:54.517Z"},"accession":"S-EPMC8267560","cross_references":{"pubmed":["34126068"],"doi":["10.1016/j.jbc.2021.100871"]}}