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Updated: Sep 18, 2025
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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
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IRF3-p300 axis controls global acetylation and mitotic progression
Won-Joo Kim1, Abdul Basit1, Eun-Bi Ko1
1Department of Biochemistry and Molecular Biology, Ajou University School of Medicine, Suwon, 443-721, South Korea; Department of Biomedical Sciences, The Graduate School, Ajou University, Suwon, 443-721, South Korea.
Biochemical and Biophysical Research Communications
|June 20, 2025
Summary
The IRF3-p300 axis regulates protein acetylation during mitosis. This pathway is crucial for cell division, with IRF3 activating p300 to control mitotic acetylation and progression.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Accurate cell division relies on regulated post-translational modifications, including lysine acetylation.
- The upstream mechanisms controlling acetylation during mitosis are not fully understood.
Purpose of the Study:
- To identify key regulators of global protein acetylation during mitosis.
- To elucidate the upstream mechanisms governing acetylation during cell division.
Main Methods:
- Investigated the role of the IRF3-p300 axis in mitotic acetylation.
- Utilized mass spectrometry to analyze the mitotic acetylome.
- Employed genetic depletion and mutant rescue experiments.
Main Results:
- Identified the IRF3-p300 axis as a major regulator of mitotic protein acetylation.
- p300 is the primary lysine acetyltransferase active during mitosis, requiring IRF3 activation.
- Loss of IRF3 or p300 impairs mitotic progression and alters the acetylation of non-histone proteins involved in RNA processing.
Conclusions:
- IRF3 acts as a non-canonical upstream activator of p300 during mitosis.
- The IRF3-p300 pathway is essential for proper mitotic progression via global regulation of protein acetylation.
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