{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["17(6)"],"submitter":["Chang CF"],"pubmed_abstract":["R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity. Despite the fact that Rspo1 holds therapeutic potential for a number of diseases, its biogenesis is not fully elucidated. All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans. Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain. Elimination of N-glycosylation at these sites affects their accumula"],"journal":["International journal of molecular sciences"],"pagination":["E937"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4926470"],"repository":["biostudies-literature"],"pubmed_title":["N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability."],"pmcid":["PMC4926470"],"pubmed_authors":["Chen CK","Wang SY","Tsai JN","Chang CF","Huang WY","Liu YY","Lin H","Hsu LS","Weng CY","Chen YH","Yuan ZX","Chou YH"],"additional_accession":[]},"is_claimable":false,"name":"N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.","description":"R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity. Despite the fact that Rspo1 holds therapeutic potential for a number of diseases, its biogenesis is not fully elucidated. All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans. Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain. Elimination of N-glycosylation at these sites affects their accumula","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jun","modification":"2025-04-22T05:03:06.74Z","creation":"2019-03-27T02:17:10Z"},"accession":"S-EPMC4926470","cross_references":{"pubmed":["27314333"],"doi":["10.3390/ijms17060937"]}}