Phosphorylation of p53 serine 15 increases interaction with CBP
PF Lambert, F Kashanchi, MF Radonovich… - Journal of Biological …, 1998 - ASBMB
p53 exerts its cell cycle regulatory effects through its ability to function as a sequence-
specific DNA binding transcription factor. CREB-binding protein (CBP)/p300, through its
interaction with the N terminus of p53, acts as a coactivator for p53 and increases the
sequence-specific DNA-binding activity of p53 by acetylating its C terminus. The same N-
terminal domain of p53 has recently been shown to be phosphorylated at Ser 15 in
response to γ-irradiation. Remarkably, we now demonstrate that phosphorylation of p53 at …
specific DNA binding transcription factor. CREB-binding protein (CBP)/p300, through its
interaction with the N terminus of p53, acts as a coactivator for p53 and increases the
sequence-specific DNA-binding activity of p53 by acetylating its C terminus. The same N-
terminal domain of p53 has recently been shown to be phosphorylated at Ser 15 in
response to γ-irradiation. Remarkably, we now demonstrate that phosphorylation of p53 at …
