{"doi":"10.1074/jbc.m003997200","title":"Complex Formation of Adenomatous Polyposis Coli Gene Product and Axin Facilitates Glycogen Synthase Kinase-3β-dependent Phosphorylation of β-Catenin and Down-regulates β-Catenin","abstract":null,"journal":"Journal of Biological Chemistry","year":2000,"id":642043,"datarank":0.7346759699926367,"base_score":4.897839799950911,"endowment":4.897839799950911,"self_citation_contribution":0.7346759699926367,"citation_network_contribution":0.0,"self_endowment_contribution":0.7346759699926367,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":133,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1525139,"name":"Hideki Yamamoto","orcid":null,"position":1,"is_corresponding":false},{"id":1669685,"name":"Michiko Kishida","orcid":null,"position":2,"is_corresponding":false},{"id":1669689,"name":"Shinji Takada","orcid":null,"position":3,"is_corresponding":false},{"id":465226,"name":"Shosei Kishida","orcid":"0000-0003-0405-851X","position":4,"is_corresponding":false},{"id":1669697,"name":"Akira Kikuchi","orcid":null,"position":5,"is_corresponding":false},{"id":1669679,"name":"Toshihide Hinoi","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Complex Formation of Adenomatous Polyposis Coli Gene Product and Axin Facilitates Glycogen Synthase Kinase-3β-dependent Phosphorylation of β-Catenin and Down-regulates β-Catenin","abstract":"Adenomatous polyposis coli gene product (APC) functions as a tumor suppressor and its mutations in familial adenomatous polyposis and colorectal cancers lead to the accumulation of cytoplasmic beta-catenin. The molecular mechanism by which APC regulates the stability of beta-catenin was investigated. The central region of APC, APC-(1211-2075), has the beta-catenin- and Axin-binding sites and down-regulates beta-catenin. Glycogen synthase kinase-3 beta (GSK-3 beta) phosphorylated beta-catenin slightly in the presence of either APC-(1211-2075) or Axin(delta)(beta)(-catenin), in which the beta-catenin-binding site is deleted, and greatly in the presence of both proteins. The enhancement of the GSK-3 beta-dependent phosphorylation of beta-catenin was eliminated by the APC-binding site of Axin. Axin down-regulated beta-catenin in SW480 cells, but not Axin(delta)(beta)(-catenin). In L cells where APC is intact, Axin(delta)(beta)(-catenin) inhibited Wnt-dependent accumulation of beta-catenin but not Axin-(298-832)(delta)(beta)(-catenin) in which the APC- and beta-catenin-binding sites are deleted. These results indicate that the complex formation of APC and Axin enhances the phosphorylation of beta-catenin by GSK-3 beta, leading to the down-regulation of beta-catenin.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"10906131","pmcid":null,"openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925820889352/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820889352?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820889352?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.M003997200","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Cell Line","Animals","Humans","Glycogen Synthase Kinases","Glycogen Synthase Kinase 3","Proteins","Cytoskeletal Proteins","Adenomatous Polyposis Coli Protein","Trans-Activators","Repressor Proteins","Ubiquitins","Down-Regulation","Mutagenesis","Binding Sites","Protein Binding","Hydrolysis","Phosphorylation","beta Catenin","Calcium-Calmodulin-Dependent Protein Kinases","Axin Protein"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-07T21:21:59.954007Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}