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Updated: Mar 30, 2026

Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage
Published on: August 21, 2021
Cross talk of tyrosine kinases with the DNA damage signaling pathways
Kiran Mahajan1, Nupam P Mahajan2
1Tumor Biology Department, Moffitt Cancer Center, 12902 Magnolia Drive, Tampa, FL 33612, USA Department of Oncological Sciences, University of South Florida, 12902 Magnolia Drive, Tampa, FL 33612, USA kiran.mahajan@moffitt.org.
Abstract:
Tyrosine kinases respond to extracellular and intracellular cues by activating specific cellular signaling cascades to regulate cell cycle, growth, proliferation, differentiation and survival. Likewise, DNA damage response proteins (DDR) activated by DNA lesions or chromatin alterations recruit the DNA repair and cell cycle checkpoint machinery to restore genome integrity and cellular homeostasis. Several new examples have been uncovered in recent studies which reveal novel epigenetic and non-epigenetic mechanisms by which tyrosine kinases interact with DDR proteins to dictate cell fate, i.e. survival or apoptosis, following DNA damage. These studies reveal the ability of tyrosine kinases to directly regulate the activity of DNA repair and cell cycle check point proteins by tyrosine phosphorylation. In addition, tyrosine kinases epigenetically regulate DNA damage signaling pathways by modifying the core histones as well as chromatin modifiers at critical tyrosine residues. Thus, deregulated tyrosine kinase driven epigenomic alterations have profound implications in cancer, aging and genetic disorders. Consequently, targeting oncogenic tyrosine kinase induced epigenetic alterations has gained significant traction in overcoming cancer cell resistance to various therapies. This review discusses mechanisms by which tyrosine kinases interact with DDR pathways to regulate processes critical for maintaining genome integrity as well as clinical strategies for targeted cancer therapies.
Insights
Tyrosine kinases and DNA damage response (DDR) proteins interact through novel epigenetic and non-epigenetic mechanisms. These interactions regulate cell fate and genome integrity, offering new therapeutic targets for cancer.
Area of Science:
- Molecular Biology
- Cellular Signaling
- Epigenetics
Background:
- Tyrosine kinases regulate cell functions via signaling cascades.
- DNA damage response (DDR) proteins maintain genome integrity.
- Interplay between tyrosine kinases and DDR is crucial for cell fate.
Purpose of the Study:
- To review novel mechanisms of tyrosine kinase and DDR protein interaction.
- To highlight epigenetic and non-epigenetic regulation in DNA damage response.
- To discuss implications for cancer therapy.
Main Methods:
- Literature review of recent studies on tyrosine kinases and DNA damage response.
- Analysis of epigenetic and non-epigenetic interaction mechanisms.
- Examination of clinical strategies targeting these pathways.
Main Results:
- Tyrosine kinases directly modulate DDR protein activity via phosphorylation.
- Tyrosine kinases epigenetically regulate DNA damage signaling by modifying histones and chromatin modifiers.
- Deregulated tyrosine kinase activity drives epigenomic alterations with implications in cancer and aging.
Conclusions:
- Tyrosine kinases and DDR pathways collaboratively control cell fate and genome maintenance.
- Targeting oncogenic tyrosine kinase-induced epigenetic alterations is a promising strategy against cancer therapy resistance.
- Understanding these interactions is key for developing novel cancer treatments.
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