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A more recent version of this article appeared on April 14, 2006
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C600001200v1
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Papers In Press, published online ahead of print February 9, 2006
J. Biol. Chem, 10.1074/jbc.C600001200
Submitted on January 4, 2006
Revised on February 8, 2006
Accepted on February 9, 2006

Estrogen receptor-alpha binds p53 tumor suppressor protein directly and represses its function

Wensheng Liu, Santhi D. Konduri, Sanjay Bansal, Bijaya K. Nayak, Sigrid A. Rajasekaran, Sankunny M. Karuppayil, Ayyappan K. Rajasekaran, and Gokul M. Das

Pharmacology & Therapeutics, Roswell Park Cancer Institute, Buffalo, NY 14263

Corresponding Author: gokul.das{at}roswellpark.org

Estrogen receptor-alpha (ERalpha ) promotes cell proliferation of breast cancer cells whereas tumor suppressor protein p53 impedes proliferation of cells with genomic damage. Whether there is a direct link between these two antagonistic pathways has remained unclear. Here we report that ERalpha binds directly to p53 and negatively regulates its function. The activation function-2 (AF-2) domain of ERalpha and the C-terminal regulatory domain of p53 are necessary for the interaction. Knocking down p53 and ERalpha by small interfering RNA (siRNA) elicits opposite effects on p53-target gene expression and cell cycle progression. Remarkably, ionizing radiation that causes genomic damage disrupts the interaction between ERalpha and p53. Ionizing radiation together with ERa knock down results in an additive effect on transcription of endogenous p53-target gene p21 (CDKN1) in human breast cancer cells. Our findings reveal a novel mechanism for regulating p53 and suggest that suppressing p53 function is an important component in the pro-proliferative role of ERalpha .


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