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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Molecular Chaperones and Protein Folding03:00

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Updated: May 17, 2026

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

HDAC inhibitors and chaperone function.

Rekha Rao1, Warren Fiskus, Siddhartha Ganguly

  • 1The University of Kansas Cancer Center, Kansas City, Kansas, USA.

Advances in Cancer Research
|October 24, 2012
PubMed
Summary
This summary is machine-generated.

Histone deacetylase inhibitors cause cancer cells to over-acetylate cellular chaperones, disrupting protein homeostasis and inducing lethal stress. This mechanism highlights their potential in cancer therapy.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Biology

Background:

  • Cellular chaperones are crucial for protein folding, maturation, and preventing aggregation.
  • Histone deacetylases (HDACs) regulate gene expression through acetylation of histones and nonhistone proteins.
  • Tumor cells heavily rely on functional chaperones for survival and proliferation.

Purpose of the Study:

  • To investigate the impact of HDAC inhibitors on chaperone acetylation and function.
  • To explore the implications of HDAC inhibitor-induced chaperone dysfunction in cancer treatment.

Main Methods:

  • Treatment of cells with HDAC inhibitors.
  • Analysis of chaperone acetylation status (e.g., HSP90, HSP70, GRP78).
  • Assessment of protein homeostasis and proteotoxic stress levels.

Main Results:

  • HDAC inhibitors induce hyperacetylation of major chaperones, including HSP90, HSP70, HSP40, and GRP78.
  • This hyperacetylation impairs chaperone function, leading to protein misfolding and proteotoxic stress.
  • Tumor cells, with their high dependence on chaperones, are particularly vulnerable to this stress.

Conclusions:

  • HDAC inhibitor-induced chaperone hyperacetylation disrupts protein homeostasis, causing lethal proteotoxic and ER stress in cancer cells.
  • This mechanism provides a rationale for using HDAC inhibitors in the treatment of solid and hematologic tumors.
  • Targeting chaperone acetylation represents a promising therapeutic strategy in oncology.