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http://purl.uniprot.org/citations/9920888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9920888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9920888http://www.w3.org/2000/01/rdf-schema#comment"Axin is a negative regulator of embryonic axis formation in vertebrates, which acts through a Wnt signal transduction pathway involving the serine/threonine kinase GSK-3 and beta-catenin. Axin has been shown to have distinct binding sites for GSK-3 and beta-catenin and to promote the phosphorylation of beta-catenin and its consequent degradation. This provides an explanation for the ability of Axin to inhibit signaling through beta-catenin. In addition, a more N-terminal region of Axin binds to adenomatous polyposis coli (APC), a tumor suppressor protein that also regulates levels of beta-catenin. Here, we report the results of a yeast two-hybrid screen for proteins that interact with the C-terminal third of Axin, a region in which no binding sites for other proteins have previously been identified. We found that Axin can bind to the catalytic subunit of the serine/threonine protein phosphatase 2A through a domain between amino acids 632 and 836. This interaction was confirmed by in vitro binding studies as well as by co-immunoprecipitation of epitope-tagged proteins expressed in cultured cells. Our results suggest that protein phosphatase 2A might interact with the Axin.APC.GSK-3.beta-catenin complex, where it could modulate the effect of GSK-3 on beta-catenin or other proteins in the complex. We also identified a region of Axin that may allow it to form dimers or multimers. Through two-hybrid and co-immunoprecipitation studies, we demonstrated that the C-terminal 100 amino acids of Axin could bind to the same region as other Axin molecules."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.6.3439"xsd:string
http://purl.uniprot.org/citations/9920888http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.6.3439"xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/author"Zeng L."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/author"Zeng L."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/author"Costantini F."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/author"Costantini F."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/author"Hsu W."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/author"Hsu W."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/pages"3439-3445"xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/pages"3439-3445"xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/title"Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/title"Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/9920888http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/9920888http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9920888
http://purl.uniprot.org/citations/9920888http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9920888
http://purl.uniprot.org/citations/9920888http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9920888
http://purl.uniprot.org/citations/9920888http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9920888