{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang X"],"funding":["NCI NIH HHS","National Institutes of Health","Susan G Komen Foundation","NIGMS NIH HHS","Jimmy V-Foundation"],"pagination":["e00609-16"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5472828"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["37(13)"],"pubmed_abstract":["The oncogenic transcription factor FoxM1 plays a vital role in cell cycle progression, is activated in numerous human malignancies, and is linked to chromosome instability. We characterize here a cullin 4-based E3 ubiquitin ligase and its substrate receptor, VprBP/DCAF1 (CRL4<sup>VprBP</sup>), which we show regulate FoxM1 ubiquitylation and degradation. Paradoxically, we also found that the substrate receptor VprBP is a potent FoxM1 activator. VprBP depletion reduces expression of FoxM1 target genes and impairs mitotic entry, whereas ectopic VprBP expression strongly activates a FoxM1 transcriptional reporter. VprBP binding to CRL4 is reduced during mitosis, and our data suggest that VprBP activation of FoxM1 is ligase independent. This implies a nonproteolytic activation mechanism that is"],"journal":["Molecular and cellular biology"],"pubmed_title":["VprBP/DCAF1 Regulates the Degradation and Nonproteolytic Activation of the Cell Cycle Transcription Factor FoxM1."],"pmcid":["PMC5472828"],"funding_grant_id":["R01GM120309","T32 GM007040","NA","P30 CA016086","CCR14298820","R01 GM120309"],"pubmed_authors":["Emanuele MJ","Zhou C","Kernan JL","Bird K","Arceci A","Wang X","Bowers A","Choudhury R","Mills CA","Bae-Jump V"],"additional_accession":[]},"is_claimable":false,"name":"VprBP/DCAF1 Regulates the Degradation and Nonproteolytic Activation of the Cell Cycle Transcription Factor FoxM1.","description":"The oncogenic transcription factor FoxM1 plays a vital role in cell cycle progression, is activated in numerous human malignancies, and is linked to chromosome instability. We characterize here a cullin 4-based E3 ubiquitin ligase and its substrate receptor, VprBP/DCAF1 (CRL4<sup>VprBP</sup>), which we show regulate FoxM1 ubiquitylation and degradation. Paradoxically, we also found that the substrate receptor VprBP is a potent FoxM1 activator. VprBP depletion reduces expression of FoxM1 target genes and impairs mitotic entry, whereas ectopic VprBP expression strongly activates a FoxM1 transcriptional reporter. VprBP binding to CRL4 is reduced during mitosis, and our data suggest that VprBP activation of FoxM1 is ligase independent. This implies a nonproteolytic activation mechanism that is","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Jul","modification":"2026-05-05T15:45:41.338Z","creation":"2019-03-27T02:47:47Z"},"accession":"S-EPMC5472828","cross_references":{"pubmed":["28416635"],"doi":["10.1128/MCB.00609-16","10.1128/mcb.00609-16"]}}