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Updated: May 26, 2026
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Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
Published on: January 31, 2018
PRDM2 and DNA damage response: phosphoregulatory signaling insights
Vaishnavi Gopalakrishnan1, Althaf Mahin1, Leona Dcunha1
1Centre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, 575018 Karnataka India.
3 Biotech
|May 25, 2026
Summary
This study maps PRDM2 phosphorylation sites and their signaling networks, revealing a strong link to DNA damage response pathways and identifying ATR as a potential kinase. This work clarifies PRDM2
Area of Science:
- Molecular Biology
- Epigenetics
- Proteomics
Background:
- PRDM2 is a histone methyltransferase crucial for gene regulation and DNA damage response.
- The functional role of PRDM2 phosphorylation is largely unknown.
- Understanding PRDM2 phosphorylation is key to elucidating its role in maintaining genomic integrity.
Purpose of the Study:
- To systematically characterize PRDM2 phosphosites and their associated signaling networks.
- To identify key PRDM2 phosphorylation sites and their regulatory partners.
- To uncover the functional implications of PRDM2 phosphorylation in cellular processes.
Main Methods:
- Large-scale cellular phosphoproteomics data analysis from PubMed-indexed articles.
- Frequency-based ranking to identify predominant PRDM2 phosphosites (Ser643, Ser421).
- Expression co-regulation analysis to map associated phospho-signaling networks and identify potential kinases (e.g., ATR).
Main Results:
- Ser643 and Ser421 identified as predominant PRDM2 phosphosites across numerous datasets.
- Over 1,251 and 715 phosphosites in other proteins co-regulated with PRDM2 Ser421 and Ser643, respectively.
- Significant enrichment of co-regulated phosphosites in cell cycle, chromatin organization, RNA processing, and DNA damage response (DDR) pathways, with strong links to DDR proteins.
Conclusions:
- A comprehensive PRDM2 phospho-signaling framework has been established.
- PRDM2 phosphorylation is strongly associated with DNA damage response pathways.
- ATR kinase is a potential regulator of PRDM2 phosphorylation, providing mechanistic insights into its network.
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