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Volume 271, Number 46, Issue of November 15, 1996 pp. 29380-29385
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Mutation of Phosphoserine 389 Affects p53 Function in Vivo

(Received for publication, June 13, 1996, and in revised form, August 30, 1996)

Mingming Hao , Andrew M. Lowy , Mini Kapoor , Abdul Deffie , Geng Liu and Guillermina Lozano

From the Department of Molecular Genetics, M. D. Anderson Cancer Center, University of Texas, Houston, Texas 77030

To study the importance of phosphorylation for p53 transactivation function, we generated mutations at each of its known phosphorylated serine amino acids. Mutations of murine p53 serine residues individually to either alanine or glutamic acid at positions 7, 9, 12, 18, 37, 312, and 389 resulted in equivalent levels of transcriptional activation in standard transient transfection experiments. However, when p53 transcriptional activity was measured in cells that attain G1 arrest upon contact inhibition, wild-type p53 was inactive, and only alteration at serine 389 to glutamic acid resulted in a functional p53 protein. This Ser right-arrow Glu mutant also has an increased ability to bind DNA. Elimination of the phosphorylation site by substitution of an alanine amino acid resulted in loss of transcriptional activity. We also demonstrated that specific phosphorylation of p53 at serine 389 is induced by cyclin E overexpression in high-density cells. Our data establish for the first time that phosphorylation of p53 at serine 389 is important in activating its function in vivo.


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