GO:0140592 histone H3R8 methyltransferase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0140592 describes the enzymatic activity that transfers a methyl group from S-adenosyl-L-methionine to arginine 8 of histone H3, producing S-adenosyl-L-homocysteine and methylated H3R8.
• The best-characterized enzyme carrying this activity is PRMT2, a type I protein arginine methyltransferase that deposits asymmetric dimethylation at H3R8 (H3R8me2a).
• H3R8me2a is a chromatin mark linked to transcriptional activation of oncogenic and inflammatory gene programs in glioblastoma, hepatocellular carcinoma and colitis [1,4,5].
• PRMT2-dependent H3R8 methylation is oxygen-sensitive; hypoxia stabilizes and enriches phosphorylated PRMT2 in transcriptional condensates to stimulate H3R8me2a deposition [2,3].
• PRMT5 also methylates H3R8 and is required for myogenesis through facilitation of ATP-dependent chromatin remodeling.
• Dysregulated H3R8 methylation contributes to cancer, neuroinflammation and inflammatory bowel disease, making this activity a candidate therapeutic target [1,2,4,5,7].
Description
GO:0140592, histone H3R8 methyltransferase activity, is a molecular function defined as the catalysis of the reaction in which S-adenosyl-L-methionine donates a methyl group to the arginine residue at position 8 of histone H3, yielding S-adenosyl-L-homocysteine and histone H3 with a methyl-arginine at position 8. This activity sits at the interface of chromatin biology and signal transduction, because the resulting mark, H3R8 methylation, can alter how nucleosomes are read by transcriptional regulators. Researchers study this term to understand how a single post-translational modification on a histone tail can reprogram gene expression in development, inflammation and cancer [1,4,5]. The principal enzyme reported to carry this activity is PRMT2, a type I protein arginine methyltransferase that deposits asymmetric dimethylation at H3R8 (H3R8me2a). In glioblastoma, PRMT2-mediated H3R8me2a is associated with oncogenic activation and tumorigenesis, and PRMT2 is oxygen-regulated, with hypoxia increasing its activity and its deposition of H3R8me2a [2,3,4]. In hepatocellular carcinoma, PRMT2 accelerates tumorigenesis by activating Bcl2 via histone H3R8 methylation. Beyond PRMT2, PRMT5 is also required for myogenesis and facilitates ATP-dependent chromatin remodeling, and PRMT5 can methylate H3R8. PRMT6 has been systematically profiled for substrate recognition and shows broad specificity with a preference for RG motifs or basic and bulky residues, informing how arginine methyltransferases select histone substrates. Because H3R8 methylation is a reversible, enzyme-written mark, it is an attractive node for experimental perturbation. Knockout, point-mutation, knock-in and overexpression models allow researchers to ask whether a candidate methyltransferase is necessary and sufficient for H3R8me2a and for downstream transcriptional and phenotypic outputs [1,4,5]. This article summarizes the definition, mechanism, key genes, disease links and research methods for GO:0140592, with all factual claims tied to the verified literature.
histone H3R8 methyltransferase activity At A Glance
| GO ID | GO:0140592 |
|---|---|
| GO term | histone H3R8 methyltransferase activity |
| Ontology | molecular_function |
| Synonym | histone H3R8 arginine methylase activity; histone H3R8 arginine methyltransferase activity; histone-H3R8 methyltransferase activity; histone methyltransferase activity (H3-R8 specific) |
| Major function | Catalyzes transfer of a methyl group from S-adenosyl-L-methionine to arginine 8 of histone H3, producing S-adenosyl-L-homocysteine and methylated H3R8 |
| Representative enzyme | PRMT2, a type I protein arginine methyltransferase that deposits asymmetric dimethylation at H3R8 (H3R8me2a) |
| Reaction direction | Methyl transfer from S-adenosyl-L-methionine to histone H3 arginine 8 |
| Substrate | Histone H3 arginine 8 |
| Cofactor | S-adenosyl-L-methionine as methyl donor |
What Is GO:0140592?
In plain terms, GO:0140592 is the activity of an enzyme that puts a methyl group onto arginine 8 of histone H3. The official definition states that it catalyzes the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 8) = S-adenosyl-L-homocysteine + (histone H3-N-methyl-arginine (position 8)), which is the addition of a methyl group to the arginine residue at position 8 of histone H3. This is a molecular_function term, not a process or a location; it describes what the enzyme does, not where or when it acts. Synonyms include histone H3R8 arginine methylase activity, histone H3R8 arginine methyltransferase activity, histone-H3R8 methyltransferase activity and histone methyltransferase activity (H3-R8 specific). The activity is carried out by protein arginine methyltransferases such as PRMT2, which uses S-adenosyl-L-methionine as the methyl donor and produces S-adenosyl-L-homocysteine as a byproduct.
Why Is histone H3R8 methyltransferase activity Important in Cell Biology?
GO:0140592 matters because the mark it writes, H3R8 methylation, is a chromatin modification that can switch gene expression programs on or off. PRMT2-dependent H3R8me2a is linked to oncogenic activation and tumorigenesis in glioblastoma, and PRMT2 is oxygen-regulated, so hypoxia can increase H3R8me2a deposition [2,3,4]. In hepatocellular carcinoma, PRMT2 accelerates tumorigenesis by activating Bcl2 via histone H3R8 methylation. In colitis, PRMT2 promotes dextran sulfate sodium-induced colitis by inhibiting the SOCS3 promoter via histone H3R8 asymmetric dimethylation. PRMT2 also has antidepressant effects that involve neuroinflammation, indicating a role beyond cancer. PRMT5, another enzyme that can methylate H3R8, is required for myogenesis because it facilitates ATP-dependent chromatin remodeling. Together, these findings make H3R8 methyltransferase activity a high-value target for mechanistic studies and for therapeutic hypothesis testing across oncology, inflammation and neuroscience [1,2,4,5,7].
• Defines a specific chromatin-writing activity that converts S-adenosyl-L-methionine into a methyl mark on histone H3 arginine 8.
• PRMT2-mediated H3R8me2a is associated with oncogenic activation and tumorigenesis in glioblastoma.
• Hypoxia increases PRMT2 activity and H3R8me2a deposition, linking oxygen sensing to chromatin methylation [2,3].
• PRMT2 promotes colitis by inhibiting the SOCS3 promoter via H3R8 asymmetric dimethylation.
• PRMT2 accelerates hepatocellular carcinoma tumorigenesis by activating Bcl2 via H3R8 methylation.
• PRMT2 has antidepressant effects that involve neuroinflammation, suggesting roles in brain disorders.
• PRMT5 is required for myogenesis and facilitates ATP-dependent chromatin remodeling, and can methylate H3R8.
• PRMT6 substrate recognition studies inform how arginine methyltransferases select histone substrates.
• The activity is a candidate target for small-molecule or genetic perturbation in cancer and inflammation [1,4,5].
• Understanding this activity helps interpret how histone arginine methylation shapes transcriptional condensates and hypoxic responses.
What Happens During histone H3R8 methyltransferase activity?
Substrate recognition and binding
In simple terms: The enzyme first finds and holds the histone H3 tail near arginine 8.
Histone H3R8 methyltransferase activity requires the enzyme to recognize the histone H3 tail and position arginine 8 in the active site. PRMT2 is the best-characterized enzyme for this activity and deposits asymmetric dimethylation at H3R8 (H3R8me2a). PRMT6 substrate recognition studies show that arginine methyltransferases can have broad specificity with a preference for RG motifs or basic and bulky residues, which helps explain how these enzymes select histone substrates. In cells, PRMT2 can be enriched in transcriptional condensates, which may concentrate enzyme and substrate to favor H3R8me2a deposition.
Methyl transfer from S-adenosyl-L-methionine
In simple terms: The enzyme takes a methyl group from a donor molecule and attaches it to arginine 8.
The catalytic step of GO:0140592 is the transfer of a methyl group from S-adenosyl-L-methionine to the arginine residue at position 8 of histone H3, producing S-adenosyl-L-homocysteine and methylated H3R8. This reaction is the defining chemistry of the term and is carried out by protein arginine methyltransferases such as PRMT2. Because the methyl donor is consumed and the byproduct S-adenosyl-L-homocysteine is generated, the activity is sensitive to cellular methylation potential and to the availability of S-adenosyl-L-methionine.
Deposition of H3R8me2a and chromatin readout
In simple terms: The new methyl mark is left on the histone, where it can change how genes are read.
PRMT2 deposits asymmetric dimethylation at H3R8, generating H3R8me2a, which is linked to oncogenic activation and tumorigenesis in glioblastoma. In hepatocellular carcinoma, PRMT2 accelerates tumorigenesis by activating Bcl2 via histone H3R8 methylation. In colitis, PRMT2 promotes dextran sulfate sodium-induced colitis by inhibiting the SOCS3 promoter via histone H3R8 asymmetric dimethylation. These examples show that the mark written by GO:0140592 can be read as an activating or repressive signal depending on the promoter and cellular context [1,4,5].
Oxygen-dependent regulation and condensate enrichment
In simple terms: Low oxygen can boost this activity by concentrating the enzyme in special compartments.
Hypoxia-inducible PRMT2 addiction has been described in glioblastomas, indicating that oxygen levels regulate PRMT2 function. Transcriptional condensates enrich phosphorylated PRMT2 to stimulate H3R8me2a deposition and the hypoxic response in glioblastoma, providing a mechanism by which the activity is spatially organized. This regulation links GO:0140592 to oxygen sensing and to the transcriptional programs that help tumors adapt to low oxygen [2,3].
Developmental and tissue-specific roles
In simple terms: This activity is also used in normal processes such as muscle formation.
PRMT5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling, and PRMT5 can methylate H3R8. This indicates that H3R8 methyltransferase activity is not only a cancer-associated function but also participates in normal differentiation programs. PRMT2 has antidepressant effects that involve neuroinflammation, suggesting additional roles in brain physiology.
Key Genes Involved in GO:0140592 histone H3R8 methyltransferase activity
The genes and proteins most directly associated with GO:0140592 are protein arginine methyltransferases and their regulatory partners, with PRMT2 as the principal enzyme for H3R8me2a and PRMT5 as an additional H3R8 methyltransferase linked to chromatin remodeling [4,6].
| Gene | Major Role | Research Relevance |
|---|---|---|
| PRMT2 | Type I protein arginine methyltransferase that deposits asymmetric dimethylation at H3R8 (H3R8me2a) | Central enzyme for GO:0140592; linked to glioblastoma, hepatocellular carcinoma, colitis and neuroinflammation [1,4,5,7] |
| PRMT5 | Protein arginine methyltransferase required for myogenesis and ATP-dependent chromatin remodeling; can methylate H3R8 | Provides a second enzyme context for H3R8 methylation and developmental chromatin remodeling |
| PRMT6 | Arginine methyltransferase with broad substrate specificity and preference for RG motifs or basic and bulky residues | Informs substrate recognition rules relevant to histone arginine methylation |
| SOCS3 | Target gene whose promoter is inhibited by PRMT2 via H3R8 asymmetric dimethylation in colitis | Readout of H3R8 methylation-dependent repression in inflammation |
| BCL2 | Target gene activated by PRMT2 via histone H3R8 methylation in hepatocellular carcinoma | Readout of H3R8 methylation-dependent activation in cancer |
| H3-8 (histone H3 arginine 8) | The substrate residue that receives the methyl group | Defines the substrate specificity of the activity |
| S-adenosyl-L-methionine | Methyl donor cofactor consumed in the reaction | Links the activity to cellular methylation potential |
| S-adenosyl-L-homocysteine | Byproduct of the methyl transfer reaction | Can be measured to monitor enzyme activity |
| Hypoxia-inducible factors (context) | Oxygen-sensing pathway that regulates PRMT2 addiction in glioblastoma | Connects GO:0140592 to hypoxic adaptation |
| Phosphorylated PRMT2 | Enriched in transcriptional condensates to stimulate H3R8me2a deposition | Explains spatial regulation of the activity |
| Transcriptional condensates | Structures that concentrate PRMT2 and substrate to favor H3R8me2a | Provide a model for how the activity is locally amplified |
| Chromatin remodeling machinery | ATP-dependent remodeling facilitated by PRMT5 during myogenesis | Links H3R8 methylation to nucleosome dynamics |
| Neuroinflammation pathway components | Mediators of PRMT2 antidepressant effects | Extend the activity beyond cancer into brain disorders |
| RG motif-containing substrates | Preferred recognition motif for some arginine methyltransferases | Guides prediction of substrate specificity |
| Basic and bulky residue contexts | Substrate features preferred by PRMT6 | Helps interpret enzyme-substrate selectivity |
How Is histone H3R8 methyltransferase activity Regulated?
GO:0140592 is regulated at multiple levels. Oxygen availability controls PRMT2 function, as hypoxia-inducible PRMT2 addiction has been described in glioblastomas. Phosphorylated PRMT2 is enriched in transcriptional condensates, which stimulates H3R8me2a deposition and the hypoxic response, indicating that post-translational modification and phase separation regulate the activity. Substrate recognition rules, including preference for RG motifs or basic and bulky residues, shape which histones and sites are methylated. The reaction itself depends on S-adenosyl-L-methionine as the methyl donor and produces S-adenosyl-L-homocysteine, so cellular methylation potential influences activity. In developmental contexts, PRMT5-dependent H3R8 methylation is coupled to ATP-dependent chromatin remodeling during myogenesis.
histone H3R8 methyltransferase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PRMT2 | Glioblastoma oncogenic activation and tumorigenesis | PRMT2 knockout or point-mutant glioblastoma cell lines with H3R8me2a readout |
| PRMT2 | Hypoxia-inducible addiction in glioblastoma | Hypoxia-treated glioblastoma cells with PRMT2 overexpression or knockdown |
| PRMT2 | Hepatocellular carcinoma via Bcl2 activation | PRMT2 knockout hepatocellular carcinoma cells with Bcl2 expression readout |
| PRMT2 | Colitis via SOCS3 promoter inhibition | PRMT2 knockout colitis models with SOCS3 promoter methylation assays |
| PRMT2 | Neuroinflammation and antidepressant effects | PRMT2 knockout or overexpression neuronal and glial models |
Glioblastoma and hypoxic adaptation
PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma. Hypoxia-inducible PRMT2 addiction in glioblastomas indicates that oxygen levels regulate this activity and that tumors may depend on it for growth. Transcriptional condensates enrich phosphorylated PRMT2 to stimulate H3R8me2a deposition and the hypoxic response, providing a mechanistic link between GO:0140592 and tumor adaptation to low oxygen.
Hepatocellular carcinoma
PRMT2 accelerates tumorigenesis of hepatocellular carcinoma by activating Bcl2 via histone H3R8 methylation. This places GO:0140592 in a pathway where a chromatin mark drives expression of an anti-apoptotic gene, supporting the idea that H3R8 methylation can promote tumor cell survival.
Inflammatory bowel disease and colitis
PRMT2 promotes dextran sulfate sodium-induced colitis by inhibiting the SOCS3 promoter via histone H3R8 asymmetric dimethylation. This demonstrates that H3R8 methylation can repress a negative regulator of inflammation, contributing to inflammatory bowel disease-like pathology.
Neuroinflammation and mood disorders
The antidepressant effects of PRMT2 involve neuroinflammation, suggesting that H3R8 methylation may modulate brain inflammatory pathways. This extends the disease relevance of GO:0140592 beyond cancer into neuropsychiatric and neuroinflammatory conditions.
From histone H3R8 methyltransferase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is PRMT2 required for H3R8me2a deposition? | PRMT2 knockout cell line with H3R8me2a immunoblot or mass spectrometry |
| Does a specific PRMT2 residue control catalytic activity? | Point-mutation knock-in of the catalytic residue with activity assays |
| Can tagged PRMT2 be used to map chromatin binding? | Tagged knock-in of PRMT2 for chromatin immunoprecipitation and imaging |
| Does PRMT2 overexpression drive oncogenic gene expression? | PRMT2 overexpression in glioblastoma or hepatocellular carcinoma cells [4,5] |
| Does PRMT2 loss reduce colitis severity? | PRMT2 knockout in dextran sulfate sodium-induced colitis models |
| Does hypoxia change PRMT2 condensate formation? | Hypoxia-treated cells with phosphorylated PRMT2 imaging [2,3] |
How to Study the histone H3R8 methyltransferase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Chromatin immunoprecipitation sequencing | Genome-wide binding of PRMT2 and H3R8me2a [1,5] | Mapping target promoters such as SOCS3 and Bcl2 [1,5] |
| Immunoblotting | Protein levels of H3R8me2a and PRMT2 | Validating knockout or overexpression effects |
| Mass spectrometry | Histone modification stoichiometry | Quantifying H3R8 methylation states |
| Transcriptional condensate imaging | Spatial enrichment of phosphorylated PRMT2 | Studying hypoxic response regulation |
| Hypoxia assays | Oxygen-dependent PRMT2 function | Testing PRMT2 addiction in glioblastoma |
| Promoter reporter assays | Transcriptional output of target genes [1,5] | Linking H3R8 methylation to gene expression [1,5] |
| Colitis models | Inflammation severity and SOCS3 promoter methylation | Testing PRMT2 role in inflammatory bowel disease |
| Myogenesis differentiation assays | PRMT5-dependent chromatin remodeling | Studying developmental roles of H3R8 methylation |
Chromatin immunoprecipitation and sequencing
Chromatin immunoprecipitation followed by sequencing can map where H3R8me2a and PRMT2 occupy the genome, revealing target promoters such as SOCS3 and Bcl2 [1,5]. This method connects the enzymatic activity of GO:0140592 to specific transcriptional outputs [1,5].
Immunoblotting and mass spectrometry for histone marks
Immunoblotting with antibodies against H3R8me2a and mass spectrometry-based histone profiling can quantify the mark written by PRMT2 and detect changes after genetic perturbation. These approaches are standard for validating whether a candidate enzyme carries GO:0140592 activity.
Transcriptional condensate imaging
Imaging of phosphorylated PRMT2 and transcriptional condensates can show how the enzyme is spatially enriched to stimulate H3R8me2a deposition and the hypoxic response. This method links subcellular organization to the activity defined by GO:0140592.
Hypoxia and oxygen-sensing assays
Hypoxia treatment combined with PRMT2 readouts can test whether oxygen availability regulates H3R8 methylation and whether tumor cells become addicted to PRMT2. Such assays connect GO:0140592 to hypoxic adaptation in glioblastoma.
How CRISPR Can Be Used to Study GO:0140592 histone H3R8 methyltransferase activity
Knockout
CRISPR knockout of PRMT2 can test whether the enzyme is required for H3R8me2a deposition and for downstream phenotypes such as glioblastoma tumorigenesis, hepatocellular carcinoma growth or colitis severity [1,4,5]. Knockout models are also useful to determine whether loss of GO:0140592 activity changes target gene expression such as SOCS3 or Bcl2 [1,5].
Point Mutation
Point mutation of the PRMT2 catalytic domain can separate the enzymatic activity of GO:0140592 from scaffolding functions of the protein. Such mutants allow researchers to ask whether methyl transfer per se is needed for oncogenic activation or for hypoxic responses [2,4].
Knock-in
Knock-in of tagged PRMT2 enables chromatin immunoprecipitation, imaging and proteomic mapping of the enzyme at endogenous expression levels. Tagged knock-in can reveal how phosphorylated PRMT2 is enriched in transcriptional condensates to stimulate H3R8me2a deposition.
Overexpression
Overexpression of PRMT2 can test sufficiency for H3R8me2a deposition and for activation of oncogenic or inflammatory gene programs [4,5]. Overexpression models are also useful in hypoxia studies to mimic PRMT2 addiction in glioblastoma.
How EDITGENE Supports histone H3R8 methyltransferase activity Research
Researchers studying histone H3R8 methyltransferase activity-related genes often need to determine whether a candidate gene is causally involved in depositing or reading the H3R8 methyl mark, and whether that activity changes disease-relevant phenotypes. EDITGENE provides the CRISPR and cell-model tools to move from correlation to causation for GO:0140592 and its associated genes such as PRMT2 [1,4,5].
Contact EDITGENE today to design your custom CRISPR model for histone H3R8 methyltransferase activity research.
Frequently Asked Questions About histone H3R8 methyltransferase activity
What is GO:0140592 histone H3R8 methyltransferase activity?
It is a molecular function describing the catalysis of methyl transfer from S-adenosyl-L-methionine to arginine 8 of histone H3, producing S-adenosyl-L-homocysteine and methylated H3R8.
What genes are involved in histone H3R8 methyltransferase activity?
PRMT2 is the principal enzyme that deposits asymmetric dimethylation at H3R8, and PRMT5 can also methylate H3R8 in the context of myogenesis and chromatin remodeling [4,6].
Which enzyme deposits H3R8me2a?
PRMT2, a type I protein arginine methyltransferase, deposits asymmetric dimethylation at H3R8 (H3R8me2a).
How is histone H3R8 methyltransferase activity regulated?
It is regulated by oxygen availability, by phosphorylation and condensate enrichment of PRMT2, and by substrate recognition rules of arginine methyltransferases [2,3,8].
What diseases are linked to H3R8 methylation?
It is linked to glioblastoma, hepatocellular carcinoma, colitis and neuroinflammation-related conditions [1,2,4,5,7].
Does PRMT2 promote cancer?
PRMT2 links H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis in glioblastoma, and accelerates hepatocellular carcinoma tumorigenesis via Bcl2 activation [4,5].
What is the role of PRMT5 in H3R8 methylation?
PRMT5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling, and it can methylate H3R8.
How can I study histone H3R8 methyltransferase activity in the lab?
Common methods include chromatin immunoprecipitation sequencing, immunoblotting, mass spectrometry, condensate imaging and hypoxia assays [1,2,3,4].
What CRISPR models are useful for studying GO:0140592?
Knockout, point-mutation, knock-in and overexpression models of PRMT2 are useful to test necessity and sufficiency for H3R8me2a and downstream phenotypes [1,3,4,5].
Why is hypoxia relevant to H3R8 methylation?
Hypoxia-inducible PRMT2 addiction occurs in glioblastomas, and transcriptional condensates enrich phosphorylated PRMT2 to stimulate H3R8me2a deposition and the hypoxic response [2,3].
Conclusion
GO:0140592, histone H3R8 methyltransferase activity, defines a specific chromatin-writing reaction carried out principally by PRMT2, with PRMT5 providing an additional context in development [4,6]. The mark it writes, H3R8me2a, is linked to oncogenic activation in glioblastoma and hepatocellular carcinoma, to colitis through SOCS3 promoter inhibition, and to neuroinflammation [1,4,5,7]. Oxygen-dependent regulation and condensate enrichment add layers of spatial and environmental control to this activity [2,3]. For researchers, the term provides a precise handle for designing experiments that test causality. Knockout, point-mutation, knock-in and overexpression models, combined with chromatin and transcriptomic readouts, can determine whether H3R8 methylation drives disease-relevant gene programs [1,3,4,5]. EDITGENE supports these workflows with CRISPR cell models, library screening and bioinformatics tailored to GO:0140592-related questions.
References
- 1. Li J et al.. 2022. Protein arginine methyltransferase 2 (PRMT2) promotes dextran sulfate sodium-induced colitis by inhibiting the SOCS3 promoter via histone H3R8 asymmetric dimethylation.. Br J Pharmacol 179(1):141-158 PMID: 34599829
- 2. Dong F et al.. 2024. Hypoxia-inducible PRMT2 addiction in glioblastomas.. Cell Signal 117:111094 PMID: 38341123
- 3. Dong F et al.. 2026. Transcriptional condensates enrich phosphorylated PRMT2 to stimulate H3R8me2a deposition and hypoxic response in glioblastoma.. Sci China Life Sci 69(1):224-238 PMID: 40926175
- 4. Dong F et al.. 2018. PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma.. Nat Commun 9(1):4552 PMID: 30382083
- 5. Hu G et al.. 2020. PRMT2 accelerates tumorigenesis of hepatocellular carcinoma by activating Bcl2 via histone H3R8 methylation.. Exp Cell Res 394(2):112152 PMID: 32574605
- 6. Dacwag CS et al.. 2007. The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling.. Mol Cell Biol 27(1):384-94 PMID: 17043109
- 7. Liu S et al.. 2024. The antidepressant effects of protein arginine methyltransferase 2 involve neuroinflammation.. Neurochem Int 176:105728 PMID: 38561150
- 8. Hamey JJ et al.. 2021. Systematic investigation of PRMT6 substrate recognition reveals broad specificity with a preference for an RG motif or basic and bulky residues.. FEBS J 288(19):5668-5691 PMID: 33764612
