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Related Concept Videos

The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Histone Modification02:32

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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
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Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
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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.
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Related Experiment Video

Updated: Nov 9, 2025

Assays for Validating Histone Acetyltransferase Inhibitors
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The STAT3 inhibitor Stattic acts independently of STAT3 to decrease histone acetylation and modulate gene expression.

Dipak K Poria1, Namratha Sheshadri1, Kuppusamy Balamurugan1

  • 1Laboratory of Cell and Developmental Signaling, Center for Cancer Research (CCR), National Cancer Institute (NCI), National Institutes of Health (NIH), Frederick, Maryland, USA.

The Journal of Biological Chemistry
|April 11, 2021
PubMed
Summary

Stattic, a STAT3 inhibitor, has significant anticancer effects independent of STAT3 inhibition. This compound reduces histone acetylation, impacting gene expression and promoting cancer cell death through epigenetic modifications.

Keywords:
STAT transcription factorTXNRD1acetylationbreastcancerhistone acetylase (HAT)histone deacetylase (HDAC)inhibitorlysine acetylase (KAT)prostate

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Research

Background:

  • Signal transducer and activator of transcription 3 (STAT3) is crucial for cellular functions and often dysregulated in cancer.
  • Stattic is widely used as a specific STAT3 inhibitor for research and therapeutic strategies.

Purpose of the Study:

  • To investigate the STAT3-independent effects of Stattic on cancer cells.
  • To reevaluate the role of Stattic in cancer research and explore its potential as a polypharmacological agent.

Main Methods:

  • Utilized STAT3-deficient (PC3) and STAT3-proficient (MDA-MB-231, SUM149) cancer cell lines.
  • Assessed Stattic's impact on histone acetylation and gene expression.
  • Evaluated Stattic's effects on autophagy and cell viability.

Main Results:

  • Stattic demonstrated STAT3-independent inhibition of histone acetylation.
  • Stattic modulated the expression of genes involved in inflammation and cancer progression (CCL20, CCL2, TNFA, CEBPD, SOX2, MYC).
  • Stattic induced autophagy and cell death, suggesting polypharmacological activity.

Conclusions:

  • Stattic exhibits significant epigenetic effects independent of STAT3 inhibition.
  • Stattic's multifaceted mechanisms, including histone acetylation modulation, contribute to its cytotoxic effects on cancer cells.
  • Reevaluation of Stattic and related compounds as polypharmacological agents is warranted for cancer therapy.