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http://purl.uniprot.org/citations/22922164http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22922164http://www.w3.org/2000/01/rdf-schema#comment"Glypicans are multifunctional proteoglycans with regulatory roles in several intercellular signaling pathways. Here, we examine the functional requirements for glypican regulation of bone morphogenetic protein (BMP)-mediated body length in C. elegans. We provide evidence that two parts of C. elegans glypican LON-2 can independently inhibit BMP signaling in vivo: the N-terminal furin protease product and the C-terminal region containing heparan sulfate attachment sequences. While the C-terminal protease product is dispensable for LON-2 minimal core protein activity, it does affect the localization of LON-2. Cleavage of LON-2 into two parts at the conserved furin protease site is not required for LON-2 to inhibit BMP-like signaling. The glycosyl-phosphatidylinositol (GPI) membrane anchor is also not absolutely required for LON-2 activity. Finally, we show that an RGD protein-protein interaction motif in the LON-2 N-terminal domain is necessary for LON-2 core protein activity, suggesting that LON-2 inhibits BMP signaling by acting as a scaffold for BMP and an RGD-binding protein."xsd:string
http://purl.uniprot.org/citations/22922164http://purl.org/dc/terms/identifier"doi:10.1016/j.ydbio.2012.08.006"xsd:string
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/author"Gumienny T.L."xsd:string
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/author"Taneja-Bageshwar S."xsd:string
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/name"Dev Biol"xsd:string
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/pages"66-76"xsd:string
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/title"Two functional domains in C. elegans glypican LON-2 can independently inhibit BMP-like signaling."xsd:string
http://purl.uniprot.org/citations/22922164http://purl.uniprot.org/core/volume"371"xsd:string
http://purl.uniprot.org/citations/22922164http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22922164
http://purl.uniprot.org/citations/22922164http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22922164
http://purl.uniprot.org/uniprot/#_Q18530-mappedCitation-22922164http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22922164
http://purl.uniprot.org/uniprot/Q18530http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22922164