Regulatory domain of protein stability of human P51/TAP63, a P53 homologue
M Osada, R Inaba, H Shinohara, M Hagiwara… - Biochemical and …, 2001 - Elsevier
M Osada, R Inaba, H Shinohara, M Hagiwara, M Nakamura, Y Ikawa
Biochemical and Biophysical Research Communications, 2001•ElsevierThe amino terminal of human P51/TAp63, a P53 homologue, possesses a transactivation
domain involved in the activation of its target genes by binding to DNA elements responsive
to the p53 protein family. Using a series of amino terminal deletions, the transactivation
domain was mapped between amino acid residues 50 to 69. This domain also regulates
protein stability in a proteasome-dependent manner, and Ser51 and Ser68 were found to be
essential for this stability. Our results suggest that P51 activity is greatly affected by protein …
domain involved in the activation of its target genes by binding to DNA elements responsive
to the p53 protein family. Using a series of amino terminal deletions, the transactivation
domain was mapped between amino acid residues 50 to 69. This domain also regulates
protein stability in a proteasome-dependent manner, and Ser51 and Ser68 were found to be
essential for this stability. Our results suggest that P51 activity is greatly affected by protein …
The amino terminal of human P51/TAp63, a P53 homologue, possesses a transactivation domain involved in the activation of its target genes by binding to DNA elements responsive to the p53 protein family. Using a series of amino terminal deletions, the transactivation domain was mapped between amino acid residues 50 to 69. This domain also regulates protein stability in a proteasome-dependent manner, and Ser51 and Ser68 were found to be essential for this stability. Our results suggest that P51 activity is greatly affected by protein stability.
Elsevier