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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

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Related Experiment Video

Updated: Jul 5, 2026

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
10:55

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Acetylation is indispensable for p53 activation.

Yi Tang1, Wenhui Zhao, Yue Chen

  • 1Institute for Cancer Genetics, College of Physicians & Surgeons, Columbia University, New York, NY 10032, USA.

Cell
|May 20, 2008
PubMed
Summary

Acetylation of the tumor suppressor p53 is essential for its activation, enabling the cellular stress response. This modification destabilizes the p53-Mdm2 interaction, promoting growth arrest and apoptosis.

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Area of Science:

  • Molecular biology
  • Cellular stress response
  • Tumor suppression

Background:

  • The tumor suppressor p53 is crucial for cellular responses to genotoxic stress.
  • p53 activation requires disruption of its interaction with the inhibitor Mdm2.
  • The precise role of p53 posttranslational modifications, like phosphorylation and acetylation, in its activation remains debated.

Purpose of the Study:

  • To identify all major acetylation sites of p53.
  • To determine if p53 acetylation is essential for its activation and function.
  • To elucidate the mechanism by which p53 acetylation influences the p53-Mdm2 interaction.

Main Methods:

  • Identification of p53 acetylation sites.
  • Analysis of p53-dependent growth arrest and apoptosis in the presence or absence of acetylation.
  • Investigation of Mdm2 recruitment to p53-responsive promoters.

Main Results:

  • Loss of p53 acetylation completely abolished p53-dependent growth arrest and apoptosis.
  • Acetylation of p53 abrogates Mdm2-mediated repression by preventing Mdm2 recruitment to target promoters.
  • p53 activation via acetylation occurs independently of its phosphorylation status.

Conclusions:

  • p53 acetylation is an indispensable event for the p53-mediated stress response.
  • Acetylation destabilizes the p53-Mdm2 interaction, leading to p53 activation.
  • This study clarifies the critical role of p53 acetylation in cellular stress response pathways.