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http://purl.uniprot.org/citations/16343438http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16343438http://www.w3.org/2000/01/rdf-schema#comment"To understand the molecular mechanism underlying HIPK2 regulation of the transcriptional activation by p53, we sought to identify the protein that interacts with HIPK2. From our yeast two-hybrid screen, we found that four and a half LIM domains 2 (FHL2) could bind to the C-terminal half of HIPK2. Further assays in yeast mapped the minimal interaction domain to amino acids 812-907 in HIPK2. The interaction was confirmed using a GST pull-down assay in vitro, and an immunoprecipitation (IP) assay and fluorescence microscopy in vivo. FHL2 alone spread throughout both the cytoplasm and nucleus but was redistributed to dot-like structures in the nucleus when HIPK2 was coexpressed in HEK293 cells. When tethered to the Gal4-responsive promoter through the Gal4 DBD fusion, FHL2 showed autonomous transcriptional activity that was enhanced by wild-type HIPK2, but not by the kinase-defective mutant. In addition, FHL2 increased the p53-dependent transcriptional activation and had an additive effect on the activation when coexpressed with HIPK2, which was again not observed with the kinase-defective mutant of HIPK2. Finally, we found a ternary complex of p53, HIPK2, and FHL2 using IP, and their recruitment to the p53-responsive p21Waf1 promoter in chromatin IP assays. Overall, our findings indicate that FHL2 can also regulate p53 via a direct association with HIPK2."xsd:string
http://purl.uniprot.org/citations/16343438http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2005.11.116"xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/author"Lee S.W."xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/author"Kim E.J."xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/author"Um S.J."xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/pages"1056-1062"xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/title"FHL2 mediates p53-induced transcriptional activation through a direct association with HIPK2."xsd:string
http://purl.uniprot.org/citations/16343438http://purl.uniprot.org/core/volume"339"xsd:string
http://purl.uniprot.org/citations/16343438http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16343438
http://purl.uniprot.org/citations/16343438http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16343438
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