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http://purl.uniprot.org/citations/17376403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17376403http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17376403http://www.w3.org/2000/01/rdf-schema#comment"Low-density lipoprotein receptor-related protein 6 (LRP6) is a component of cell-surface receptors for Wnt proteins and Wnt is known to promote recruitment of Axin by LRP6 thereby inhibiting beta-catenin's degradation. We show here that growth factor receptor-bound protein10 (GRB10), a multi-modular adaptor protein that is known to associate with several transmembrane tyrosine kinase receptors, binds to the intracellular portion of LRP6 and negatively regulates Wnt signaling. GRB10 overexpression suppressed Wnt3a-, and LRP6-induced but not beta-catenin-induced TCF-dependent-reporter activities in HEK293T cells, suggesting that GRB10 functions upstream of beta-catenin. Actually, GRB10 overexpression attenuated the Wnt3a-induced accumulation of beta-catenin. In addition, RNAi-mediated down-regulation of endogenous GRB10 stimulated Wnt3a-induced reporter activities, indicating that GRB10 is indeed a novel negative regulator of the Wnt signaling pathway. The finding that GRB10 interferes with the binding of Axin to LRP6 indicated a possible molecular mechanism by which the overexpression of GRB10 suppresses Wnt signaling."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2007.03.019"xsd:string
http://purl.uniprot.org/citations/17376403http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2007.03.019"xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/author"Brown A.M."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/author"Brown A.M."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/author"Yanagawa S."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/author"Yanagawa S."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/author"Tezuka N."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/author"Tezuka N."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/pages"648-654"xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/pages"648-654"xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/title"GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt signaling pathway."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/title"GRB10 binds to LRP6, the Wnt co-receptor and inhibits canonical Wnt signaling pathway."xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/volume"356"xsd:string
http://purl.uniprot.org/citations/17376403http://purl.uniprot.org/core/volume"356"xsd:string
http://purl.uniprot.org/citations/17376403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17376403
http://purl.uniprot.org/citations/17376403http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17376403
http://purl.uniprot.org/citations/17376403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17376403
http://purl.uniprot.org/citations/17376403http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17376403