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Cited by 423

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Phosphorylation of p53 Serine 15 Increases Interaction with CBP

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Lambert, Paul F., Kashanchi, Fatah, Radonovich, Michael F., Shiekhattar, Ramin, Brady, John N.·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.49.33048
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Abstract

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 Ser15 in response to gamma-irradiation. Remarkably, we now demonstrate that phosphorylation of p53 at Ser15 increases its ability to recruit CBP/p300. The increase in CBP/p300 binding was followed by an increase in the overall level of acetylation of the C terminus of p53. These results provide a mechanism for the activation of p53-regulated genes following DNA damage, through a signaling pathway linking p53 N-terminal kinase and C-terminal acetyltransferase activities.

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Metadata

Authors
Lambert, P. F., Kashanchi, F., Radonovich, M. F., Shiekhattar, R., & Brady, J. N.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-12
Volume
273
Issue
49
Pages
33048-33053
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.273.49.33048
OpenAlex
W2045552152
Cited by
423
References
6
FWCI
10.83
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: Phosphorylation of p53 Serine 15 Increases Interaction with CBP. https://app.cochat.ai/papers/10.1074/jbc.273.49.33048
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Lambert, P. F., Kashanchi, F., Radonovich, M. F., Shiekhattar, R., & Brady, J. N. (1998). Phosphorylation of p53 Serine 15 Increases Interaction with CBP. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.49.33048

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