Abstract
The protein arginine methyltransferases (PRMTs) are involved in such biological processes as transcription regulation, DNA repair, RNA splicing, and signal transduction, etc. In this study, we mainly focused on PRMT5, a member of the type II PRMTs, which functions mainly alongside other interacting proteins. PRMT5 has been shown to be overexpressed in a wide variety of cancers and other diseases, and is involved in the regulation of Epstein-Barr virus infection, viral carcinogenesis, spliceosome, hepatitis B, cell cycles, and various signaling pathways. We analyzed the regulatory roles of PRMT5 and interacting proteins in various biological processes above-mentioned, to elucidate for the first time the interaction between PRMT5 and its interacting proteins. This systemic analysis will enrich the biological theory and contribute to the development of novel therapies.
Highlights
Protein post-translational modification (PTM) is critical for proteome diversification, which contributes to the regulation of protein function and cell signal transduction
Based on the above PRMT5 Interacting Proteins (PIPs), we found 155 proteins that were listed in at least two databases
PRMT5 depletion caused an increase of sub-G1 cells during the DNA damage response, simultaneously, compared with wild-type p53, a p53 mutant compromised in arginine methylation may affect the cell cycle (Radzisheuskaya et al, 2019)
Summary
Protein post-translational modification (PTM) is critical for proteome diversification, which contributes to the regulation of protein function and cell signal transduction. The inhibition of PRMT5-mediated H3K27 methylation contributes to cell cycle progression (Liu F. et al, 2020).
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