Cited by 752Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysCell death mechanisms and regulation

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Acetylation of the p53 DNA-binding domain regulates apoptosis induction.

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Sykes, Stephen M., Mellert, Hestia S., Holbert, Marc A., Li, Keqin, Marmorstein, Ronen, Lane, William S., McMahon, Steven B.·2006·Molecular Cell

DOI 10.1016/j.molcel.2006.11.026PMC PMC1766330

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Abstract

The ability of p53 to induce apoptosis plays an important role in tumor suppression. Here, we describe a previously unknown posttranslational modification of the DNA-binding domain of p53. This modification, acetylation of lysine 120 (K120), occurs rapidly after DNA damage and is catalyzed by the MYST family acetyltransferases hMOF and TIP60. Mutation of K120 to arginine, as occurs in human cancer, debilitates K120 acetylation and diminishes p53-mediated apoptosis without affecting cell-cycle arrest. The K120R mutation selectively blocks the transcription of proapoptotic target genes such as BAX and PUMA while the nonapoptotic targets p21 and hMDM2 remain unaffected. Consistent with this, depletion of hMOF and/or TIP60 inhibits the ability of p53 to activate BAX and PUMA transcription. Furthermore, the acetyllysine 120 (acetyl-K120) form of p53 specifically accumulates at proapoptotic target genes. These data suggest that K120 acetylation may help distinguish the cell-cycle arrest and apoptotic functions of p53.

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Role of novel histone modifications in cancer
Shanmugam, M. K., Arfuso, F., Arumugam, S., Chinnathambi, A., Jinsong, B., Warrier, S. R., Wang, L. Z., Kumar, A. P., Ahn, K. S., Sethi, G., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.23356 · Cited by 132

Authors: Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B.
Affiliations: Thomas Jefferson University (US)
The Wistar Institute (US)
Harvard University (US)
Corresponding author: McMahon, Steven B.
ORCID: Sykes, Stephen M.
Marmorstein, Ronen
McMahon, Steven B.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2006-12
Volume: 24
Issue: 6
Pages: 841-851
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2006.11.026
PMC: PMC1766330
OpenAlex: W2038324148
Cited by: 752
References: 51
Citations by year: 2026: 22 · 2025: 28 · 2024: 25 · 2023: 24 · 2022: 31 · 2021: 39 · 2020: 29 · 2019: 30 · 2018: 38 · 2017: 31 · 2016: 43 · 2015: 44 · 2014: 45 · 2013: 52 · 2012: 52
FWCI: 21.33
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2456 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Cancer Institute (R01CA090465, CA090465, CA098172, R01CA098172)
National Institute of General Medical Sciences (R01GM060293)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords: p53, DNA-binding domain, post-translational modification, apoptosis induction, hMOF, Tip60, p21, DNA damage response, tumor suppression, cell cycle arrest
MeSH terms: Lysine Acetyltransferase 5, Acetylation, Amino Acid Sequence, Binding Sites, Cell Cycle, Humans, Molecular Sequence Data, Promoter Regions, Genetic, Proto-Oncogene Proteins, Tumor Suppressor Protein p53, Apoptosis, Apoptosis Regulatory Proteins, bcl-2-Associated X Protein, Histone Acetyltransferases

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Acetylation of the p53 DNA-binding domain regulates apoptosis induction.

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