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J. Biol. Chem., Vol. 277, Issue 26, 23493-23499, June 28, 2002

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E2F-3B Is a Physiological Target of Cyclin A^*

Yiwen He and W. Douglas Cress^§¶

From the  Department of Biochemistry and Molecular Biology, ^§ Department of Interdisciplinary Oncology, University of South Florida, College of Medicine, and ^¶ Program in Molecular Oncology, H. Lee Moffitt Comprehensive Cancer Center and Research Institute, Tampa, Florida 33612

The E2F family of transcription factors controls the expression of numerous genes that are required for the G₁/S transition. Among the mechanisms that modulate the activity of the E2F proteins, cyclin A has been found to be important for the down-regulation of E2F-1, -2, and -3A activity after cells have progressed through G₁/S. Specifically, phosphorylation of these E2F proteins by cyclin A/Cdk2 ultimately results in their necessary degradation as cells progress through S phase. E2F-3B was recently identified as an alternatively spliced form of E2F-3A that was predicted to lack a functional cyclin A binding domain. In this paper, we present considerable evidence that contradicts this prediction. First, we demonstrate binding of cyclin A to E2F-3B as bacterially expressed proteins in vitro. Second, we demonstrate binding of cyclin A to E2F-3B in mammalian cells in vivo. Third, we show that co-expression of cyclin A with E2F-3B significantly reduces E2F-3B-mediated transcriptional activity. Finally, in synchronized cells, we observe down-regulation of E2F-3B protein expression coincident with the up-regulation of cyclin A. We conclude that E2F-3B is a physiological target of cyclin A.

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