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http://purl.uniprot.org/citations/17108107http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17108107http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17108107http://www.w3.org/2000/01/rdf-schema#comment"The tumor suppressor LKB1 is an evolutionarily conserved serine/threonine kinase. In humans, LKB1 can be inactivated either by germ-line mutations resulting in Peutz-Jeghers syndrome or by somatic mutations causing predisposition to multiple sporadic cancers. LKB1 has wide-ranging functions involved in tumor suppression and cell homeostasis, including establishing cell polarity, setting energy metabolic balance (via phosphorylation of AMP-dependent kinase), regulating the cell cycle, and promoting apoptosis. LKB1 function was previously linked to the tumor suppressor p53 and shown to activate the p53 target gene p21/WAF1. In this study, we further investigated LKB1 activation of the p21/WAF1 gene and addressed whether LKB1 is directly involved at the gene promoter. We find that, consistent with previous studies, LKB1 stabilizes p53 in vivo, correlating with activation of p21/WAF1. We show that LKB1 physically associates with p53 in the nucleus and directly or indirectly phosphorylates p53 Ser15 (previously shown to be phosphorylated by AMP-dependent kinase) and p53 Ser392. Further, these two p53 residues are required for LKB1-dependent cell cycle G(1) arrest. Chromatin immunoprecipitation analyses show that LKB1 is recruited directly to the p21/WAF1 promoter, as well as to other p53 activated promoters, in a p53-dependent fashion. Finally, a genetic fusion of LKB1 to defective p53, deleted for its activation domains, promotes activation of p21/WAF1. These results indicate that LKB1 has a direct role in activation of p21/WAF1 gene."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.org/dc/terms/identifier"doi:10.1158/0008-5472.can-06-0999"xsd:string
http://purl.uniprot.org/citations/17108107http://purl.org/dc/terms/identifier"doi:10.1158/0008-5472.can-06-0999"xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/author"Berger S.L."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/author"Berger S.L."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/author"Zeng P.Y."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/author"Zeng P.Y."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/name"Cancer Res."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/name"Cancer Res."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/pages"10701-10708"xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/pages"10701-10708"xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/title"LKB1 is recruited to the p21/WAF1 promoter by p53 to mediate transcriptional activation."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/title"LKB1 is recruited to the p21/WAF1 promoter by p53 to mediate transcriptional activation."xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/17108107http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/17108107http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17108107
http://purl.uniprot.org/citations/17108107http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17108107
http://purl.uniprot.org/citations/17108107http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17108107
http://purl.uniprot.org/citations/17108107http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17108107
http://purl.uniprot.org/uniprot/Q15831http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17108107
http://purl.uniprot.org/uniprot/P04637http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17108107