Critical Roles of Protein Arginine Methylation in the Central Nervous System

Chang, Ke-Wei; Gao, Dan; Jin, Yan; Lin, Liyan; Cui, Tingting; Lu, Shemin

doi:10.1007/s12035-023-03465-x

Cited by 9 publications

(4 citation statements)

References 238 publications

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“…Similar to other PTM-related kinases, PRMTs methylate the arginine residues of both histone and non-histone proteins, playing essential roles in gene regulation, genome stability maintenance, RNA maturation, and cellular stress-responsive signaling [1][2][3]41]. Importantly, the abnormally high expression of certain PRMTs also indicates their involvement in numerous diseases, such as tumorigenesis, neurodegeneration, and inflammation, as extensively reviewed elsewhere [13,14].…”

Section: Arginine Methylation Of Histones and Non-histonesmentioning

confidence: 99%

“…The substrate range and biological functions of arginine methylation in cancer, neurological disorders, and inflammatory diseases have been extensively discussed [2,13,14]. A myriad of distinct PTMs are deployed by viral infections as connectors in virus-host interactions [15,16].…”

Section: Protein Arginine Methylationmentioning

confidence: 99%

“…Additionally, PRMTs methylate proteins from multiple layers of the DNA damage response, such as BRCA1 (Breast cancer susceptibility gene 1), 53BP1 (p53 binding protein 1), and MRE11 (meiotic recombination 11), regulating their transcription, stability, activity, subcellular location, and protein or nucleic acid interactions to adapt to genotoxic stimuli [80][81][82]. Furthermore, PRMT-mediated arginine methylation has been implicated in several diseases, including cancer, neurodegenerative disorders, and inflammatory diseases, because of the wide range of functional substrates and biological processes involved [13,14]. Extensive research has been conducted on the potential regulatory functions of PRMTs in these diseases, offering promising therapeutic avenues, the details of which are not discussed herein.…”

Section: Non-histone Methylation By Prmtsmentioning

confidence: 99%

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Protein arginine methylation in viral infection and antiviral immunity

Zheng,

Chen,

Ren

et al. 2023

Int. J. Biol. Sci.

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Protein arginine methyltransferase (PRMT)-mediated arginine methylation is an important post-transcriptional modification that regulates various cellular processes including epigenetic gene regulation, genome stability maintenance, RNA metabolism, and stress-responsive signal transduction. The varying substrates and biological functions of arginine methylation in cancer and neurological diseases have been extensively discussed, providing a rationale for targeting PRMTs in clinical applications. An increasing number of studies have demonstrated an interplay between arginine methylation and viral infections. PRMTs have been found to methylate and regulate several host cell proteins and different functional types of viral proteins, such as viral capsids, mRNA exporters, transcription factors, and latency regulators. This modulation affects their activity, subcellular localization, protein-nucleic acid and protein-protein interactions, ultimately impacting their roles in various virus-associated processes. In this review, we discuss the classification, structure, and regulation of PRMTs and their pleiotropic biological functions through the methylation of histones and non-histones. Additionally, we summarize the broad spectrum of PRMT substrates and explore their intricate effects on various viral infection processes and antiviral innate immunity. Thus, comprehending the regulation of arginine methylation provides a critical foundation for understanding the pathogenesis of viral diseases and uncovering opportunities for antiviral therapy.

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Section: Arginine Methylation Of Histones and Non-histonesmentioning

confidence: 99%

Section: Protein Arginine Methylationmentioning

confidence: 99%

Section: Non-histone Methylation By Prmtsmentioning

confidence: 99%

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Protein arginine methylation in viral infection and antiviral immunity

Zheng,

Chen,

Ren

et al. 2023

Int. J. Biol. Sci.

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“…Arginine methylation has been found to regulate a wide range of biological processes, including DNA damage repair, transcription, splicing, cell signaling, and cell cycles. − They are involved in many human diseases such as cancers and inflammatory-related diseases. − Arginine methylation is catalyzed by protein arginine methyltransferases (PRMTs), which transfer the methyl group from S -adenosyl- l -methionine (SAM) to the guanidinium group. To date, humans are known to have nine PRMTs, which are further categorized into three types according to their methylation products (Figure ).…”

Section: Arginine Modificationsmentioning

confidence: 99%

Orthogonal Translation for Site-Specific Installation of Post-translational Modifications

Gan,

Fan

2024

Chem. Rev.

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Post-translational modifications (PTMs) endow proteins with new properties to respond to environmental changes or growth needs. With the development of advanced proteomics techniques, hundreds of distinct types of PTMs have been observed in a wide range of proteins from bacteria, archaea, and eukarya. To identify the roles of these PTMs, scientists have applied various approaches. However, high dynamics, low stoichiometry, and crosstalk between PTMs make it almost impossible to obtain homogeneously modified proteins for characterization of the site-specific effect of individual PTM on target proteins. To solve this problem, the genetic code expansion (GCE) strategy has been introduced into the field of PTM studies. Instead of modifying proteins after translation, GCE incorporates modified amino acids into proteins during translation, thus generating site-specifically modified proteins at target positions. In this review, we summarize the development of GCE systems for orthogonal translation for site-specific installation of PTMs.

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Reexamining the diverse functions of arginine in biochemistry

Gupta,

Uversky

2024

Biochemical and Biophysical Research Communications

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Critical Roles of Protein Arginine Methylation in the Central Nervous System

Cited by 9 publications

References 238 publications

Protein arginine methylation in viral infection and antiviral immunity

Protein arginine methylation in viral infection and antiviral immunity

Orthogonal Translation for Site-Specific Installation of Post-translational Modifications

Reexamining the diverse functions of arginine in biochemistry

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