Evidence map›Paper›PMID 17189187›Full record

ArticleMolecular cell2006

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

Stephen M Sykes, Hestia S Mellert, Marc A Holbert, Keqin Li, Ronen Marmorstein, William S Lane, Steven B McMahon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 437 papers.

0numbers the graph read from it
0cells of the map it votes in
437citing papers in PubMed
18.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

437 citing papers in PubMed, 735 citations in OpenAlex.

  1. Review
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377 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Stephen M SykesKimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Hestia S Mellert
Marc A Holbert
Keqin Li
Ronen Marmorstein
William S Lane
Steven B McMahon
The Wistar Institute · USSidney Kimmel Cancer Center · USThomas Jefferson University · USUniversity of Pennsylvania · US

Funding

Structure/Function of Histone AcetyltransferasesR01GM060293 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN · 2000 to 2016
$5.3M
Functional analysis of transcriptional program regulated by the c-MYC oncoproteinR01CA090465 · NCI · WISTAR INSTITUTE · PI MCMAHON, STEVEN B. · 2002 to 2012
$2.9M
Role of TRRAP in the p53-Mediated Transcription of mdm2R01CA098172 · NCI · WISTAR INSTITUTE · PI MCMAHON, STEVEN B · 2003 to 2007
$1.4M
NCI NIH HHS CA090465NCI NIH HHS CA098172NCI NIH HHS R01 CA090465NCI NIH HHS R01 CA098172NIGMS NIH HHS R01 GM060293
6 · The paper itself

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.

Indexed as

ApoptosisAcetylationAmino Acid SequenceApoptosis Regulatory Proteinsbcl-2-Associated X ProteinBinding SitesCell CycleHistone AcetyltransferasesHumansLysine Acetyltransferase 5Molecular Sequence DataPromoter Regions, GeneticProto-Oncogene ProteinsTumor Suppressor Protein p53Apoptosis Regulatory ProteinsBBC3 protein, humanbcl-2-Associated X ProteinHistone AcetyltransferasesKAT5 protein, humanKAT8 protein, humanLysine Acetyltransferase 5Proto-Oncogene ProteinsTumor Suppressor Protein p53

Identifiers

PMID17189187
PMCPMC1766330
OpenAlexW2038324148

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.