Related Experiment Video
Updated: Feb 2, 2026

05:44
Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
Published on: January 26, 2024
1.3K
Characterization of FOXO Acetylation.
Shang Yao1, Zimam Mahmud1, Nikoleta Sachini1,2,3
1Department of Surgery and Cancer, Imperial College London, Imperial Centre for Translational and Experimental Medicine (ICTEM), London, UK.
Methods in Molecular Biology (Clifton, N.J.)
|November 11, 2018
Summary
Forkhead box O3 (FOXO3) is a tumor suppressor. Targeting sirtuin proteins may offer new breast cancer treatment strategies by affecting FOXO3 inactivation.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Forkhead box O3 (FOXO3) acts as a tumor suppressor, regulating critical cellular processes like cell cycle, apoptosis, and metabolism.
- Inactivation of FOXO3 is linked to cancer development and progression.
- Sirtuin proteins can inactivate FOXO3 through deacetylation at the posttranslational level.
Purpose of the Study:
- To investigate the role of sirtuin proteins in controlling FOXO3 posttranslational modifications.
- To establish methods for studying sirtuin-mediated FOXO3 regulation in cancer cells.
- To explore potential therapeutic strategies targeting sirtuin-FOXO3 interactions in breast cancer.
Main Methods:
- Description of three distinct experimental procedures.
- Focus on studying posttranslational modifications of FOXO3.
- Utilizing cancer cell models to investigate sirtuin protein activity.
Main Results:
- The study outlines methodologies for analyzing FOXO3 modifications.
- The procedures allow for the examination of sirtuin-dependent FOXO3 regulation.
- These methods are applicable to cancer cell research.
Conclusions:
- Understanding sirtuin-mediated FOXO3 inactivation is crucial for cancer research.
- Targeting sirtuin proteins presents a potential therapeutic avenue for breast cancer.
- The described procedures facilitate further investigation into FOXO3 regulation in cancer.
Related Concept Videos
Phase II Reactions: Acetylation Reactions
813
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...
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...
813
Euchromatin
8.9K
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
8.9K
Pyruvate Oxidation
168.8K
After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
168.8K
Covalently Linked Protein Regulators
9.6K
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....
These groups modify specific amino acids in a protein....
9.6K
Co-activators and Co-repressors
8.6K
Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
8.6K
Dietary Connections
61.9K
In biological systems, most metabolic pathways are interconnected. The cellular respiration processes that convert glucose to ATP—such as glycolysis, pyruvate oxidation, and the citric acid cycle—tie into those that break down other organic compounds. As a result, various foods—from apples to cheese to guacamole—end up as ATP. In addition to carbohydrates, food also contains proteins and lipids—such as cholesterol and fats. All of these organic compounds are used...
61.9K

