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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.
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...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...

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Related Experiment Video

Updated: May 19, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
08:31

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

Published on: April 10, 2020

Identifying acetylated proteins in mitosis.

Carol Chuang1, Li-yuan Yu-Lee

  • 1Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.

Methods in Molecular Biology (Clifton, N.J.)
|August 21, 2012
PubMed
Summary

Histone deacetylase inhibitors impact anticancer therapy. This study identifies novel mitotic protein acetylation targets regulated by HDAC3, enhancing our understanding of non-genomic roles in cell division.

Area of Science:

  • Cell Biology
  • Proteomics
  • Molecular Biology

Background:

  • Histone deacetylase (HDAC) inhibitors are utilized in cancer therapy targeting gene transcription.
  • The role of HDACs in protein acetylation beyond genomic targets, particularly during mitosis, remains largely unexplored.
  • HDAC3 has been identified as a key regulator of mitotic progression when localized on the mitotic spindle.

Purpose of the Study:

  • To investigate potential non-histone protein targets of HDACs during mitosis.
  • To identify acetylated proteins involved in mitosis using a proteomics approach.
  • To explore the regulatory role of HDAC3 in mitotic protein acetylation.

Main Methods:

  • Cell synchronization in mitosis followed by anti-acetyl-lysine immunoprecipitation.

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Last Updated: May 19, 2026

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Published on: January 8, 2018

  • Identification of acetylated proteins using Liquid Chromatography-Electrospray Ionization-Tandem Mass Spectrometry (LC-ESI-MS/MS).
  • Validation of protein acetylation using Western blot analysis and reciprocal immunoprecipitation experiments.

    • Main Results:

    • A subset of mitotic proteins was identified as acetylated.
    • The acetylation status of several mitotic proteins was confirmed.
    • Treatment with apicidin, an HDAC3 inhibitor, enhanced the acetylation of specific mitotic proteins, suggesting HDAC3 regulation.

    Conclusions:

    • HDAC3 plays a role in regulating the acetylation of non-histone proteins during mitosis.
    • This study expands the known functions of HDACs to include the regulation of mitotic protein acetylation.
    • NudC is presented as an example of an acetylated protein sensitive to apicidin treatment during mitosis.