E2FBP1/DRIL1, an AT-rich interaction domain-family transcription factor, is regulated by p53

• Published in: Molecular cancer research Vol. 1; no. 6; pp. 438 - 444
• Main Authors: KAIWEN MA, ARAKI, Keigo, ICHWAN, Solachuddin J. A, SUGANUMA, Tamaki, TAMAMORI-ADACHI, Mimi, IKEDA, Masa-Aki
• Format: Journal Article
• Language: English
• Published: Philadelphia, PA American Association for Cancer Research 01.04.2003
• Subjects: AT Rich Sequence - genetics; Base Sequence; Biological and medical sciences; Cell differentiation, maturation, development, hematopoiesis; Cell Division; Cell Line, Tumor; Cell physiology; Cyclin D1 - metabolism; DNA Damage; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Introns - genetics; Molecular and cellular biology; Molecular Sequence Data; Oncogenes - genetics; Protein Binding; Protein Structure, Tertiary; RNA, Messenger - genetics; RNA, Messenger - metabolism; Trans-Activators; Transcription Factors; Transcription, Genetic - genetics; Tumor Suppressor Protein p53 - metabolism
• ISSN: 1541-7786; 1557-3125

E2FBP1/DRIL1 is an AT-rich interaction domain DNA-binding protein and is ubiquitously expressed in various tissues. It has been shown that Bright, the mouse orthologue of E2FBP1/DRIL1, exhibits sequence-specific DNA binding and regulates immunoglobulin transcription. Here we show a novel connection between E2FBP1/DRIL1 and the p53 tumor suppressor, a key regulator of growth arrest or apoptosis in response to cellular stress. We found a putative p53-binding site, which specifically responded to p53, in the second intron of the E2FBP1/DRIL1 gene. E2FBP1/DRIL1was induced by p53 and up-regulated following DNA damage caused by UV radiation or doxorubicin treatment in a manner dependent on endogenous p53. The ectopic expression of E2FBP1/DRIL1 induced growth arrest in U2OS cells expressing normal p53, but not Saos-2 cells lacking p53. These results suggest that E2FBP1/DRIL1 may play a role in growth suppression mediated by p53.