Serine-arginine protein kinases and their targets in viral infection and their inhibition

Zheng, Kai; Ren, Zhe; Wang, Yifei

doi:10.1007/s00018-023-04808-6

Cited by 3 publications

(4 citation statements)

References 171 publications

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“…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 . Accumulating evidence illustrates the pleiotropic roles of PRMTs and arginine methylation in diverse cellular and viral infection-associated processes.…”

Section: Protein Arginine Methylationmentioning

confidence: 99%

“…ICP27 induces the nuclear accumulation of serine-arginine protein kinase 1 (SRPK1) and inhibits its phosphatase activity, leading to the hypophosphorylation of splicing factors (SR proteins). This ultimately results in the failure of host spliceosome assembly, facilitating viral transcription and replication (Figure 6 A) 16 , 120 . Subsequently, ICP27 disperses from the transcription site and acts as an mRNA export factor/chaperone.…”

Section: Prmts Regulate Viral Infectionmentioning

confidence: 99%

“…It does so by inhibiting viral protein synthesis through sequestration of the SG nucleation factor, G3BP1 151 . Notably, cellular phosphatases such as SRPK1 and glycogen synthase kinase 3 can phosphorylate the central RG-rich linker region, affecting the aforementioned functions of the N protein 16 , 152 , 153 . In addition, arginine methylation by PRMT affects protein-protein and protein-RNA interactions with the N protein, which are necessary for viral production 154 .…”

Section: Prmts Regulate Viral Infectionmentioning

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: Protein Arginine Methylationmentioning

confidence: 99%

Section: Prmts Regulate Viral Infectionmentioning

confidence: 99%

Section: Prmts Regulate Viral Infectionmentioning

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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“…Among substrates for protein kinases and protein phosphatases are proteins from both RNA and DNA viruses, and their phosphorylation forms an essential step in the viral life cycle [17][18][19][20][21][22]. Phosphorylation/dephosphorylation is mediated by cellular protein kinases/phosphatases, but some viruses encode their own protein kinases and protein phosphatases [23][24][25][26][27][28].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field

Moens,

Passerini,

Falquet

et al. 2023

Viruses

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Protein phosphorylation and dephosphorylation are the most common post-translational modifications mediated by protein kinases and protein phosphatases, respectively. These reversible processes can modulate the function of the target protein, such as its activity, subcellular localization, stability, and interaction with other proteins. Phosphorylation of viral proteins plays an important role in the life cycle of a virus. In this review, we highlight biological implications of the phosphorylation of the monkey polyomavirus SV40 large T and small t antigens, summarize our current knowledge of the phosphorylation of these proteins of human polyomaviruses, and conclude with gaps in the knowledge and a proposal for future research directions.

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Psr1 phosphatase regulates pre‐mRNA splicing through spliceosomal B complex factor Snu66

Varikkapulakkal,

Pillai,

Mishra

2024

The FEBS Journal

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Regulated precursor messenger RNA (pre‐mRNA) splicing modulates gene expression and promotes alternative splicing. The process is regulated by modifications of spliceosomal proteins and small nuclear RNAs (snRNAs). Here, we show that the protein phosphatase Psr1, known for its plasma membrane localisation and function in general stress response in Saccharomyces cerevisiae, also plays a regulatory role in pre‐mRNA splicing. Independently of its presence at the plasma membrane, Psr1 binds and dephosphorylates the core splicing factor Snu66. The enzyme is not an integral component of the spliceosome. Psr1 deletion in yeast, or tethering of its catalytic mutant to Snu66, results in splicing defects of introns with non‐canonical 5′ splice sites (ss). While the Psr1 binding site on Snu66 is distinct from the Hub1 interaction domains (HIND), Hub1 displaces Psr1 from Snu66. Thus, Psr1 phosphatase plays a regulatory role in pre‐mRNA splicing by modulating Snu66 functions.

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Serine-arginine protein kinases and their targets in viral infection and their inhibition

Cited by 3 publications

References 171 publications

Protein arginine methylation in viral infection and antiviral immunity

Protein arginine methylation in viral infection and antiviral immunity

Phosphorylation of Human Polyomavirus Large and Small T Antigens: An Ignored Research Field

Psr1 phosphatase regulates pre‐mRNA splicing through spliceosomal B complex factor Snu66

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