Abstract 2411 Oligomerization of Protein Arginine Methyltransferase 1 and its functional impact on substrate arginine methylation

Protein arginine methyltransferases 1 (PRMT1) is a critical enzyme that engages in post-translational modification activity in mammalian cells. It regulates multiple cellular pathways such as gene transcription, RNA splicing, and signal transduction. Conversely, dysregulation of PRMT1 correlates to cancer development in colorectal cancer, carcinoma, and leukemia. Prior studies have demonstrated the importance of dimerization for PRMT1 enzymatic activity. However, there is a lack of research on PRMT1 higher-order oligomer formation and its function.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109290
Primary Topic
Cancer-related gene regulation
Type
article
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Abstract 2411 Oligomerization of Protein Arginine Methyltransferase 1 and its functional impact on substrate arginine methylation

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article

Abstract 2411 Oligomerization of Protein Arginine Methyltransferase 1 and its functional impact on substrate arginine methylation

Eswar Kumar Nadendla, Mengtong Cao, Elizabeth Oladoyin Agboluaje, May P. Xiong, Tanmoy Paul, Chunli Yan, Tran Dang, Sunil Tripath
article en

Abstract

Protein arginine methyltransferases 1 (PRMT1) is a critical enzyme that engages in post-translational modification activity in mammalian cells. It regulates multiple cellular pathways such as gene transcription, RNA splicing, and signal transduction. Conversely, dysregulation of PRMT1 correlates to cancer development in colorectal cancer, carcinoma, and leukemia. Prior studies have demonstrated the importance of dimerization for PRMT1 enzymatic activity. However, there is a lack of research on PRMT1 higher-order oligomer formation and its function.

Journal of Biological ChemistryVol. 301(5)
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Cancer-related gene regulation
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