Arginine Methylation of NIP45 Modulates Cytokine Gene Expression in Effector T Lymphocytes

Mowen, Kerri; Schurter, Brandon T.; Fathman, John W.; David, Michael; Glimcher, Laurie H.

doi:10.1016/j.molcel.2004.06.042

Cited by 122 publications

(130 citation statements)

References 51 publications

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“…[Color figure can be viewed in the online issue, which is available at www.interscience.wiley.com.] (Mowen et al, 2004). Methylated NIP-45 heterodimerizes with NFAT and enhances NFAT driven cytokine production upon TCR signaling (Mowen et al, 2004).…”

Section: Protein Arginine Methyltransferasesmentioning

confidence: 99%

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Interplay between chromatin remodelers and protein arginine methyltransferases

Pal

Sif

2007

Journal Cellular Physiology

139

124

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Chromatin modifying enzymes have emerged as key regulators of all DNA based processes, which control cell growth, development, and differentiation. Recently, it has become clear that different chromatin remodeling and histone-modifying activities are involved in transcriptional activation and repression. Among the enzymes involved in regulating chromatin structure is the family of protein arginine methyltransferases (PRMTs) that specializes in methylating both histones as well as key cellular proteins. There are eleven different PRMT genes (PRMT1-11) whose biological function remains under explored. PRMTs regulate various cellular processes such as DNA repair and transcription, RNA processing, signal transduction, and nucleo-cytoplasmic localization. Like histone lysine methylation, methylation of histone arginine residues can either induce or inhibit transcription depending on the residue being modified and the type of methylation being introduced. In this review, we will focus on the latest findings and biological roles of ATP-dependent chromatin remodeling complexes and PRMT enzymes, and how their aberrant expression is linked to cancer.

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Section: Protein Arginine Methyltransferasesmentioning

confidence: 99%

“…(Mowen et al, 2004). Methylated NIP-45 heterodimerizes with NFAT and enhances NFAT driven cytokine production upon TCR signaling (Mowen et al, 2004). In the case of nuclear receptor HNF4, PRMT1 activates transcription through two mechanisms (Barrero and Malik, 2006).…”

Section: Protein Arginine Methyltransferasesmentioning

confidence: 99%

Interplay between chromatin remodelers and protein arginine methyltransferases

Pal

Sif

2007

Journal Cellular Physiology

139

124

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“…PRMT1, on the one hand, can catalyze the methylation of histones H4 at arginine 3 (H4R3), which acts as a part of the histone code to regulate gene expression (11)(12)(13); on the other hand, recent studies have revealed that a plethora of proteins with methylated arginine residues catalyzed by PRMT1 implicate in a variety of cellular processes. For example, PRMT1 enhances gene transcription by methylating N-terminal arginine residues in NFAT-interacting protein 45, which heterodimerizes with NFAT and then enhances NFAT, driving cytokine production upon TCR signaling of T cells (14,15).…”

mentioning

confidence: 99%

Upregulated Protein Arginine Methyltransferase 1 by IL-4 Increases Eotaxin-1 Expression in Airway Epithelial Cells and Participates in Antigen-Induced Pulmonary Inflammation in Rats

Sun

Yang

Zhong

et al. 2012

The Journal of Immunology

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Protein arginine methyltransferases (PRMTs), catalyzing methylation of both histones and other cellular proteins, have emerged as key regulators of various cellular processes. This study aimed to identify key PRMTs involved in Ag-induced pulmonary inflammation (AIPI), a rat model for asthma, and to explore the role of PRMT1 in the IL-4–induced eosinophil infiltration process. E3 rats were i.p. sensitized with OVA/alum and intranasally challenged with OVA to induce AIPI. The expressions of PRMT1–6, eotaxin-1, and CCR3 in lungs were screened by real-time quantitative PCR. Arginine methyltransferase inhibitor 1 (AMI-1, a pan-PRMT inhibitor) and small interfering RNA–PRMT1 were used to interrupt the function of PRMT1 in A549 cells. In addition, AMI-1 was administrated intranasally to AIPI rats to observe the effects on inflammatory parameters. The results showed that PRMT1 expression was mainly expressed in bronchus and alveolus epithelium and significantly upregulated in lungs from AIPI rats. The inhibition of PRMTs by AMI-1 and the knockdown of PRMT1 expression were able to downregulate the expressions of eotaxin-1 and CCR3 with the IL-4 stimulation in the epithelial cells. Furthermore, AMI-1 administration to AIPI rats can also ameliorate pulmonary inflammation, reduce IL-4 production and humoral immune response, and abrogate eosinophil infiltration into the lungs. In summary, PRMT1 expression is upregulated in AIPI rat lungs and can be stimulated by IL-4. Intervention of PRMT1 activity can abrogate IL-4–dependent eotaxin-1 production to influence the pulmonary inflammation with eosinophil infiltration. The findings may provide experimental evidence that PRMT1 plays an important role in asthma pathogenesis.

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“…In general, methylation of the arginine residue is thought to regulate protein-protein and protein-nucleic acid interactions potentially by increasing its ''hydrophobic'' character (Boisvert et al 2005). Methylation of arginine residues occurs also in other chromatin proteins involved in cytokine signaling, like the PRMT1-driven methylation of the arginine-glycine rich N terminus of the coactivator NIP45, which promotes the association between NIP45 and the transcription factor NFAT and results in an augmented activity of the IL-4 and IFNg gene promoter (Mowen et al 2004).…”

Section: Discussionmentioning

confidence: 99%

PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling

Weber¹,

Maass²,

Schuemann³

et al. 2009

Genes Dev.

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To elucidate the function of the transcriptional coregulator PRMT1 (protein arginine methyltranferase 1) in interferon (IFN) signaling, we investigated the expression of STAT1 (signal transducer and activator of transcription) target genes in PRMT1-depleted cells. We show here that PRMT1 represses a subset of IFNginducible STAT1 target genes in a methyltransferase-dependent manner. These genes are also regulated by the STAT1 inhibitor PIAS1 (protein inhibitor of activated STAT1). PIAS1 is arginine methylated by PRMT1 in vitro as well as in vivo upon IFN treatment. Mutational and mass spectrometric analysis of PIAS1 identifies Arg 303 as the single methylation site. Using both methylation-deficient and methylation-mimicking mutants, we find that arginine methylation of PIAS1 is essential for the repressive function of PRMT1 in IFN-dependent transcription and for the recruitment of PIAS1 to STAT1 target gene promoters in the late phase of the IFN response. Methylation-dependent promoter recruitment of PIAS1 results in the release of STAT1 and coincides with the decline of STAT1-activated transcription. Accordingly, knockdown of PRMT1 or PIAS1 enhances the antiproliferative effect of IFNg. Our findings identify PRMT1 as a novel and crucial negative regulator of STAT1 activation that controls PIAS1-mediated repression by arginine methylation.[Keywords: Transcriptional repression; interferon signaling; STAT1; PIAS1; PRMT1; arginine methylation] Supplemental material is available at http://www.genesdev.org.

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Arginine Methylation of NIP45 Modulates Cytokine Gene Expression in Effector T Lymphocytes

Cited by 122 publications

References 51 publications

Interplay between chromatin remodelers and protein arginine methyltransferases

Interplay between chromatin remodelers and protein arginine methyltransferases

Upregulated Protein Arginine Methyltransferase 1 by IL-4 Increases Eotaxin-1 Expression in Airway Epithelial Cells and Participates in Antigen-Induced Pulmonary Inflammation in Rats

PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling

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