Twist and p53 reciprocally regulate target genes via direct interaction View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2008-05-26

AUTHORS

M Shiota, H Izumi, T Onitsuka, N Miyamoto, E Kashiwagi, A Kidani, G Hirano, M Takahashi, S Naito, K Kohno

ABSTRACT

Twist is basic helix-loop-helix transcription factor that binds to E-boxes in gene promoters. Twist possesses an oncogenic function by interfering with the tumor suppressor function of p53. Using a membrane pull-down assay, we found that Twist directly interacts with p53 and that this interaction underlies the inhibitory effects on p53 target gene expression. Twist interacted with the DNA-binding domain of p53 and suppressed the DNA-binding activity of p53. Transcriptional activation of the p21 promoter by p53 was significantly repressed by the expression of Twist. On the other hand, p53 interacted with the N-terminal domain of Twist and repressed Twist-dependent YB-1 promoter activity. Importantly, we found that p53-dependent growth suppression was canceled by the expression of either Twist or YB-1. Thus, our data suggest that Twist inhibits p53 function via a direct interaction with p53. More... »

PAGES

5543-5553

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/onc.2008.176

DOI

http://dx.doi.org/10.1038/onc.2008.176

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011620128

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/18504427


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