This Article Full Text Full Text (PDF) Supplementary Data Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zhang, Y. Articles by Band, V. Search for Related Content PubMed PubMed Citation Articles by Zhang, Y. Articles by Band, V.

The Human Orthologue of Drosophila Ecdysoneless Protein Interacts with p53 and Regulates Its Function

¹ Divisions of Cancer Biology and ² Molecular Oncology, Department of Medicine, Evanston Northwestern Healthcare Research Institute and Feinberg School of Medicine, and ³ Robert H. Lurie Comprehensive Cancer Center, and ⁴ Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois; and ⁵ Massachusetts General Hospital, Cutaneous Biology Research Center, Charlestown, Massachusetts

Requests for reprints: Vimla Band, Division of Cancer Biology, Evanston Northwestern Healthcare Research Institute, 1001 University Place, Evanston, IL 60201. Phone: 224-364-7501; Fax: 224-364-7402; E-mail: v-band{at}northwestern.edu.

Biochemical mechanisms that control the levels and function of key tumor suppressor proteins are of great interest as their alterations can lead to oncogenic transformation. Here, we identify the human orthologue of Drosophila melanogaster ecdysoneless (hEcd) as a novel p53-interacting protein. Overexpression of hEcd increases the levels of p53 and enhances p53 target gene transcription whereas hEcd knockdown has the opposite effects on p53 levels and target gene expression. Furthermore, hEcd interacts with murine double minute-2 and stabilizes p53 by inhibiting murine double minute-2–mediated degradation of p53. Thus, hEcd protein represents a novel regulator of p53 stability and function. Our studies also represent the first demonstration of a biochemical function for hEcd protein and raise the possibility that altered hEcd levels and/or function may contribute to oncogenesis. (Cancer Res 2006; 66(14): 7167-75)

This article has been cited by other articles:

				hEcd, a p53 Regulator Cancer Res., September 15, 2006; 66(18): 9338 - 9338. [Full Text] [PDF]