Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Histone Modification02:32

Histone Modification

15.9K
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...
15.9K
Histone Modification02:32

Histone Modification

4.4K
4.4K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

9.3K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
9.3K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.9K
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
4.9K
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

7.3K
Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
7.3K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.7K
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....
8.7K
  1. Home
  3. A Cancer-specific Antigen Drives Histone Acetylation By Stabilizing The Acetyltransferases.
  1. Home
  3. A Cancer-specific Antigen Drives Histone Acetylation By Stabilizing The Acetyltransferases.

Related Experiment Video

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

7.0K

A cancer-specific antigen drives histone acetylation by stabilizing the acetyltransferases.

Xuekun Fu1, Xu Yang2, Jie Huang3

  • 1Department of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055, China.

Cell Reports
|October 8, 2025

View abstract on PubMed

Summary
This summary is machine-generated.

Cancer protein MAGE-A10 stabilizes histone acetyltransferases (KAT2A/2B) by blocking their degradation, increasing histone acetylation. This MAGE-A10/KAT2A feedback loop promotes tumorigenesis, offering potential therapeutic targets.

Keywords:
CP: CancerCP: Molecular biologyKAT2AKAT2BMAGE-A10cancerubiquitintion

More Related Videos

Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
05:44

Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening

Published on: January 26, 2024

1.3K
Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

562

Related Experiment Videos

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

7.0K
Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
05:44

Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening

Published on: January 26, 2024

1.3K
Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

562

Area of Science:

  • Molecular Biology
  • Cancer Biology
  • Epigenetics

Background:

  • Histone acetylation regulates gene expression and chromatin structure.
  • Histone acetyltransferases (HATs) maintain acetylation homeostasis; their disruption is linked to cancer.
  • Aberrant gene expression and cancer development arise from disrupted acetylation balance.

Purpose of the Study:

  • To investigate the role of cancer-specific protein MAGE-A10 in regulating histone acetylation.
  • To elucidate the molecular mechanisms by which MAGE-A10 influences HAT stability and function.
  • To identify potential therapeutic strategies targeting the MAGE-A10 pathway in cancer.

Main Methods:

  • Investigated MAGE-A10's interaction with KAT2A and KAT2B.
  • Analyzed MAGE-A10's effect on KAT2A/2B degradation via p62-mediated autophagy.
  • Examined MAGE-A10's influence on the CUL4A-DDB1 E3 ubiquitin ligase complex.
  • Assessed the feedback loop between KAT2A and MAGE-A10 transcription.

    • Main Results:

    • MAGE-A10 stabilizes KAT2A and KAT2B, increasing cellular histone acetylation.
    • MAGE-A10 prevents KAT2A/2B degradation by inhibiting their ubiquitination via the CUL4A-DDB1 complex.
    • A positive feedback loop exists where KAT2A enhances MAGE-A10 transcription, contributing to tumorigenesis.

    Conclusions:

    • MAGE-A10 hijacks cellular machinery to increase histone acetylation in cancer.
    • The MAGE-A10-mediated stabilization of HATs promotes aberrant gene expression driving cancer.
    • Targeting the MAGE-A10 pathway may offer novel therapeutic avenues for cancer treatment.