| http://purl.uniprot.org/citations/15526030 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15526030 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15526030 | http://www.w3.org/2000/01/rdf-schema#comment | "Axin and p53 are tumor suppressors, controlling cell growth, apoptosis, and development. We show that Axin interacts with homeodomain-interacting protein kinase-2 (HIPK2), which is linked to UV-induced p53-dependent apoptosis by interacting with, and phosphorylating Ser 46 of, p53. In addition to association with p53 via HIPK2, Axin contains a separate domain that directly interacts with p53 at their physiological concentrations. Axin stimulates p53-dependent reporter transcription in 293 cells, but not in 293T, H1299, or SaOS-2 cells that are defective in p53 signaling. Axin, but not AxindeltaHIPK2, activates HIPK2-mediated p53 phosphorylation at Ser 46, facilitating p53-dependent transcriptional activity and apoptosis. Specific knockdown of Axin by siRNA reduced UV-induced Ser-46 phosphorylation and apoptosis. Kinase-dead HIPK2 reduced Axin-induced p53-dependent transcriptional activity, indicating that Axin stimulates p53 function through HIPK2 kinase activity. Interestingly, HIPK2deltaAxin that lacks its Axin-binding region acts as a dominant-positive form in p53 activation, suggesting that the Axin-binding region of HIPK2 is a putative autoinhibitory domain. These results show that Axin acts as a tumor suppressor by facilitating p53 function through integration of multiple factors."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7600475"xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.emboj.7600475"xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Han J."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Han J."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Lin S."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Lin S."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Li P."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Li P."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Li Q."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Li Q."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Wu Z."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Wu Z."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Xu Z."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Xu Z."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Ye Z."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Ye Z."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Lin S.-C."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Lin S.-C."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Luo W."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Luo W."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Rui Y."xsd:string |
| http://purl.uniprot.org/citations/15526030 | http://purl.uniprot.org/core/author | "Rui Y."xsd:string |