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http://purl.uniprot.org/citations/10207085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10207085http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10207085http://www.w3.org/2000/01/rdf-schema#comment"p120(ctn) is an Armadillo repeat domain protein with structural similarity to the cell adhesion cofactors beta-catenin and plakoglobin. All three proteins interact directly with the cytoplasmic domain of the transmembrane cell adhesion molecule E-cadherin; beta-catenin and plakoglobin bind a carboxy-terminal region in a mutually exclusive manner, while p120 binds the juxtamembrane region. Unlike beta-catenin and plakoglobin, p120 does not interact with alpha-catenin, the tumor suppressor adenomatous polyposis coli (APC), or the transcription factor Lef-1, suggesting that it has unique binding partners and plays a distinct role in the cadherin-catenin complex. Using p120 as bait, we conducted a yeast two-hybrid screen and identified a novel transcription factor which we named Kaiso. Kaiso's deduced amino acid sequence revealed an amino-terminal BTB/POZ protein-protein interaction domain and three carboxy-terminal zinc fingers of the C2H2 DNA-binding type. Kaiso thus belongs to a rapidly growing family of POZ-ZF transcription factors that include the Drosophila developmental regulators Tramtrak and Bric à brac, and the human oncoproteins BCL-6 and PLZF, which are causally linked to non-Hodgkins' lymphoma and acute promyelocytic leukemia, respectively. Monoclonal antibodies to Kaiso were generated and used to immunolocalize the protein and confirm the specificity of the p120-Kaiso interaction in mammalian cells. Kaiso specifically coprecipitated with a variety of p120-specific monoclonal antibodies but not with antibodies to alpha- or beta-catenin, E-cadherin, or APC. Like other POZ-ZF proteins, Kaiso localized to the nucleus and was associated with specific nuclear dots. Yeast two-hybrid interaction assays mapped the binding domains to Arm repeats 1 to 7 of p120 and the carboxy-terminal 200 amino acids of Kaiso. In addition, Kaiso homodimerized via its POZ domain but it did not heterodimerize with BCL-6, which heterodimerizes with PLZF. The involvement of POZ-ZF proteins in development and cancer makes Kaiso an interesting candidate for a downstream effector of cadherin and/or p120 signaling."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.org/dc/terms/identifier"doi:10.1128/mcb.19.5.3614"xsd:string
http://purl.uniprot.org/citations/10207085http://purl.org/dc/terms/identifier"doi:10.1128/mcb.19.5.3614"xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/author"Daniel J.M."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/author"Daniel J.M."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/author"Reynolds A.B."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/author"Reynolds A.B."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/pages"3614-3623"xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/pages"3614-3623"xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/title"The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/title"The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor."xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10207085http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10207085http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10207085
http://purl.uniprot.org/citations/10207085http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10207085
http://purl.uniprot.org/citations/10207085http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10207085
http://purl.uniprot.org/citations/10207085http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10207085
http://purl.uniprot.org/uniprot/P30999http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10207085
http://purl.uniprot.org/uniprot/Q8BN78http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10207085