{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu J"],"funding":["Swiss National Science Foundation"],"pagination":["1344"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12897804"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(3)"],"pubmed_abstract":["The transcription factor <i>DMP1</i> is a positive regulator of the tumor suppressor ARF, which in turn controls cell-cycle progression and/or apoptosis through p53. Given the role of DMP1 in the ARF-p53 pathway, we investigated whether the p53 transcription factor might regulate DMP1 expression. We found that endogenous human <i>(h)DMP1</i> mRNA levels were significantly decreased upon induction of the temperature-sensitive p53<sup>Val135</sup> in normal fibroblasts. Consistent with this observation, a p53 knockdown in MCF7 breast cancer cells resulted in increased <i>hDMP1</i> mRNA and protein levels. At the molecular level, we found that p53 directly repressed the hDMP1 promoter activity by up to 90%. This repression was not mediated by p53 binding to the two putative p53-binding sites "],"journal":["International journal of molecular sciences"],"pubmed_title":["Identification of DMP1 as Novel p53 Repressed Transcriptional Target."],"pmcid":["PMC12897804"],"funding_grant_id":["173219","310030","31003A_173219","197786","310030_197786"],"pubmed_authors":["Zlobec I","Torbett BE","Arvidsson G","Tschan MP","Britschgi C","Krauer D","Xu J"],"additional_accession":[]},"is_claimable":false,"name":"Identification of DMP1 as Novel p53 Repressed Transcriptional Target.","description":"The transcription factor <i>DMP1</i> is a positive regulator of the tumor suppressor ARF, which in turn controls cell-cycle progression and/or apoptosis through p53. Given the role of DMP1 in the ARF-p53 pathway, we investigated whether the p53 transcription factor might regulate DMP1 expression. We found that endogenous human <i>(h)DMP1</i> mRNA levels were significantly decreased upon induction of the temperature-sensitive p53<sup>Val135</sup> in normal fibroblasts. Consistent with this observation, a p53 knockdown in MCF7 breast cancer cells resulted in increased <i>hDMP1</i> mRNA and protein levels. At the molecular level, we found that p53 directly repressed the hDMP1 promoter activity by up to 90%. This repression was not mediated by p53 binding to the two putative p53-binding sites ","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-08T03:12:39.446Z","creation":"2026-07-08T03:08:30.384Z"},"accession":"S-EPMC12897804","cross_references":{"pubmed":["41683766"],"doi":["10.3390/ijms27031344"]}}