RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/27881714http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27881714http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27881714http://www.w3.org/2000/01/rdf-schema#comment"Glycosylphosphatidylinositol-anchored proteins (GPI-APs) can be shed from the cell membrane by GPI cleavage. In this study, we report a novel GPI-processing enzyme, termed post-glycosylphosphatidylinositol attachment to proteins 6 (PGAP6), which is a GPI-specific phospholipase A2 mainly localized at the cell surface. CRIPTO, a GPI-AP, which plays critical roles in early embryonic development by acting as a Nodal coreceptor, is a highly sensitive substrate of PGAP6, whereas CRYPTIC, a close homologue of CRIPTO, is not sensitive. CRIPTO processed by PGAP6 was released as a lysophosphatidylinositol-bearing form, which is further cleaved by phospholipase D. CRIPTO shed by PGAP6 was active as a coreceptor in Nodal signaling, whereas cell-associated CRIPTO activity was reduced when PGAP6 was expressed. Homozygous Pgap6 knockout mice showed defects in early embryonic development, particularly in the formation of the anterior-posterior axis, which are common features with Cripto knockout embryos. These results suggest PGAP6 plays a critical role in Nodal signaling modulation through CRIPTO shedding."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201605121"xsd:string
http://purl.uniprot.org/citations/27881714http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201605121"xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Fujita M."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Fujita M."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Ikawa M."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Ikawa M."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Maeda Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Saito K."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Saito K."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Takada Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Takada Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Hamada H."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Hamada H."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Lee G.H."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Lee G.H."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Fujihara Y."xsd:string
http://purl.uniprot.org/citations/27881714http://purl.uniprot.org/core/author"Fujihara Y."xsd:string