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Zeitschriftenartikel zum Thema „Prmt4/carm1“

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Veröffentlicht am 12. April 2025

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1

Wang, Shu-Ching Mary, Dennis H. Dowhan, Natalie A. Eriksson, and George E. O. Muscat. "CARM1/PRMT4 is necessary for the glycogen gene expression programme in skeletal muscle cells." Biochemical Journal 444, no. 2 (2012): 323–31. http://dx.doi.org/10.1042/bj20112033.

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CARM1 (co-activator-associated arginine methyltransferase 1)/PRMT4 (protein arginine methyltransferase 4), functions as a co-activator for transcription factors that are regulators of muscle fibre type and oxidative metabolism, including PGC (peroxisome-proliferator-activated receptor γ co-activator)-1α and MEF2 (myocyte enhancer factor 2). We observed significantly higher Prmt4 mRNA expression in comparison with Prmt1–Prmt6 mRNA expression in mouse muscle (in vitro and in vivo). Transfection of Prmt4 siRNA (small interfering RNA) into mouse skeletal muscle C2C12 cells attenuated PRMT4 mRNA an
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Dacwag, Caroline S., Mark T. Bedford, Saïd Sif, and Anthony N. Imbalzano. "Distinct Protein Arginine Methyltransferases Promote ATP-Dependent Chromatin Remodeling Function at Different Stages of Skeletal Muscle Differentiation." Molecular and Cellular Biology 29, no. 7 (2009): 1909–21. http://dx.doi.org/10.1128/mcb.00742-08.

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ABSTRACT Temporal regulation of gene expression is a hallmark of cellular differentiation pathways, yet the mechanisms controlling the timing of expression for different classes of differentiation-specific genes are not well understood. We previously demonstrated that the class II arginine methyltransferase Prmt5 was required for skeletal muscle differentiation at the early stages of myogenesis (C. S. Dacwag, Y. Ohkawa, S. Pal, S. Sif, and A. N. Imbalzano, Mol. Cell. Biol. 27:384-394, 2007). Specifically, when Prmt5 levels were reduced, the ATP-dependent SWI/SNF chromatin-remodeling enzymes co
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Ito, Tatsuo, Neelu Yadav, Jaeho Lee, et al. "Arginine methyltransferase CARM1/PRMT4 regulates endochondral ossification." BMC Developmental Biology 9, no. 1 (2009): 47. http://dx.doi.org/10.1186/1471-213x-9-47.

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Gunnell, Emma A., Alaa Al-Noori, Usama Muhsen, Clare C. Davies, James Dowden, and Ingrid Dreveny. "Structural and biochemical evaluation of bisubstrate inhibitors of protein arginine N-methyltransferases PRMT1 and CARM1 (PRMT4)." Biochemical Journal 477, no. 4 (2020): 787–800. http://dx.doi.org/10.1042/bcj20190826.

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Attenuating the function of protein arginine methyltransferases (PRMTs) is an objective for the investigation and treatment of several diseases including cardiovascular disease and cancer. Bisubstrate inhibitors that simultaneously target binding sites for arginine substrate and the cofactor (S-adenosylmethionine (SAM)) have potential utility, but structural information on their binding is required for their development. Evaluation of bisubstrate inhibitors featuring an isosteric guanidine replacement with two prominent enzymes PRMT1 and CARM1 (PRMT4) by isothermal titration calorimetry (ITC),
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Selvi, B. Ruthrotha, Amrutha Swaminathan, Uma Maheshwari, Ananthamurthy Nagabhushana, Rakesh K. Mishra, and Tapas K. Kundu. "CARM1 regulates astroglial lineage through transcriptional regulation of Nanog and posttranscriptional regulation by miR92a." Molecular Biology of the Cell 26, no. 2 (2015): 316–26. http://dx.doi.org/10.1091/mbc.e14-01-0019.

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Coactivator-associated arginine methyltransferase (CARM1/PRMT4)–mediated transcriptional coactivation and arginine methylation is known to regulate various tissue-specific differentiation events. Although CARM1 is expressed in the neural crest region in early development, coinciding with early neuronal progenitor specification, the role of CARM1 in any neuronal developmental pathways has been unexplored. Using a specific small-molecule inhibitor of CARM1-mediated H3R17 methylation in human embryonic stem cell line, we find that H3R17 methylation contributes to the maintenance of the astroglial
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Batut, Julie, Carine Duboé, and Laurence Vandel. "The Methyltransferases PRMT4/CARM1 and PRMT5 Control Differentially Myogenesis in Zebrafish." PLoS ONE 6, no. 10 (2011): e25427. http://dx.doi.org/10.1371/journal.pone.0025427.

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Vu, Ly P., Xinyang Zhao, Fabiana Perna, and Stephen D. Nimer. "Regulation of AML1/RUNX1 Function by Protein Arginine Methyltransferase 4 (PRMT4) in Myeloid Differentiation." Blood 118, no. 21 (2011): 549. http://dx.doi.org/10.1182/blood.v118.21.549.549.

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Abstract Abstract 549 RUNX1 (also known as AML1) is the DNA binding component of the Core Binding Factor (CBF)-transcriptional regulatory complex, which plays an important role in hematopoiesis. Upon binding to the common binding sequence -PyGpyGGTPy (Py = pyrimidine) in the regulatory regions of promoters and enhancers of its target genes, RUNX1 acts either as an activator or a repressor, depending on promoter context and its interacting partners. Thus, modulation of the network of RUNX1 interactions can influence hematopoiesis. However, how RUNX1 selects one set of partners over another to a
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Suresh, Samyuktha, Solène Huard, and Thierry Dubois. "CARM1/PRMT4: Making Its Mark beyond Its Function as a Transcriptional Coactivator." Trends in Cell Biology 31, no. 5 (2021): 402–17. http://dx.doi.org/10.1016/j.tcb.2020.12.010.

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Gao, Wei-wei, Rong-quan Xiao, Bing-ling Peng та ін. "Arginine methylation of HSP70 regulates retinoid acid-mediated RARβ2 gene activation". Proceedings of the National Academy of Sciences 112, № 26 (2015): E3327—E3336. http://dx.doi.org/10.1073/pnas.1509658112.

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Although “histone” methyltransferases and demethylases are well established to regulate transcriptional programs and to use nonhistone proteins as substrates, their possible roles in regulation of heat-shock proteins in the nucleus have not been investigated. Here, we report that a highly conserved arginine residue, R469, in HSP70 (heat-shock protein of 70 kDa) proteins, an evolutionarily conserved protein family of ATP-dependent molecular chaperone, was monomethylated (me1), at least partially, by coactivator-associated arginine methyltransferase 1/protein arginine methyltransferase 4 (CARM1/
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Mookhtiar, Adnan K., Sarah Greenblatt, Na Man, et al. "CARM1 Inhibition: Evaluation of Response and Efficacy in Acute Myeloid Leukemia." Blood 132, Supplement 1 (2018): 2719. http://dx.doi.org/10.1182/blood-2018-99-114981.

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Abstract Small molecule protein arginine methyltransferase inhibitors (PRMTi) are being actively pursued for the treatment of a variety of cancers; however, the mechanisms of response to PRMTi remain poorly understood. CARM1, also known as PRMT4, is significantly overexpressed in AML, as well as many solid tumors, and regulates myeloid differentiation. We have shown the dependency of AML cells, but not normal blood cells, on CARM1 activity, based on CARM1 knockout, CARM1 knockdown, and chemical inhibition (Greenblatt et al. Cancer Cell 2018). These experiments showed that CARM1 regulates essen
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Quintero, Cynthia M., Kristian B. Laursen, Nigel P. Mongan, Minkui Luo, and Lorraine J. Gudas. "CARM1 (PRMT4) Acts as a Transcriptional Coactivator during Retinoic Acid-Induced Embryonic Stem Cell Differentiation." Journal of Molecular Biology 430, no. 21 (2018): 4168–82. http://dx.doi.org/10.1016/j.jmb.2018.08.014.

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Steiner, Laurie A., Yelena Maksimova, Vincent Schulz, and Patrick G. Gallagher. "A Common Regulatory Signature Associated with Barrier Insulators in Human Primary Erythroid Cells." Blood 116, no. 21 (2010): 3868. http://dx.doi.org/10.1182/blood.v116.21.3868.3868.

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Abstract Abstract 3868 Insulators are DNA sequences and associated binding proteins that establish and/or maintain boundaries between regions of active and silenced chromatin domains. In higher organisms, there are 2 types of insulators, enhancer-blocking insulators, which establish chromatin domains to separate enhancers and promoters, and barrier insulators, which create a barrier to protect against heterochromatin-mediated gene silencing. Despite their role as critical regulators of tissue-specific gene expression, barrier insulators are poorly understood in mammalian cells, with much of ou
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Lai, Yandong, Xiuying Li, Tiao Li, et al. "Endotoxin stabilizes protein arginine methyltransferase 4 (PRMT4) protein triggering death of lung epithelia." Cell Death & Disease 12, no. 9 (2021). http://dx.doi.org/10.1038/s41419-021-04115-7.

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AbstractLung epithelial cell death is a prominent feature of acute lung injury and acute respiratory distress syndrome (ALI/ARDS), which results from severe pulmonary infection leading to respiratory failure. Multiple mechanisms are believed to contribute to the death of epithelia; however, limited data propose a role for epigenetic modifiers. In this study, we report that a chromatin modulator protein arginine N-methyltransferase 4/coactivator-associated arginine methyltransferase 1 (PRMT4/CARM1) is elevated in human lung tissues with pneumonia and in experimental lung injury models. Here PRM
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Huang, Jiezuo, Beining Qiao, Yixin Yuan, et al. "PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer." Journal of Cellular and Molecular Medicine 29, no. 4 (2025). https://doi.org/10.1111/jcmm.70386.

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ABSTRACTThe family of protein arginine methyltransferases (PRMTs) occupies an important position in biology, especially during the initiation and development of cancer. PRMT3 and CARM1(also known as PRMT4), being type I protein arginine methyltransferases, are key in controlling tumour progression by catalysing the mono‐methylation and asymmetric di‐methylation of both histone and non‐histone substrates. This paper reviews the functions and potential therapeutic target value of PRMT3 and CARM1 in a variety of cancers. Studies have identified abnormal expressions of PRMT3 and CARM1 in several m
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Milite, Ciro, Giuliana Sarno, Ida Pacilio, et al. "Prodrug Approach to Exploit (S) Alanine as Arginine Mimic Moiety in the Development of Protein Arginine Methyltransferase 4 Inhibitors." ChemMedChem, May 16, 2024. http://dx.doi.org/10.1002/cmdc.202400139.

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Protein arginine methyltransferase (PRMT) 4 (also known as coactivator‐associated arginine methyltransferase 1; CARM1) is involved in a variety of biological processes and is considered as an emerging target class in oncology and other diseases. A successful strategy to identify PRMT substrate‐competitive inhibitors has been to exploit chemical scaffolds able to mimic the arginine substrate. (S)‐Alanine amide moiety is a valuable arginine mimic for the development of potent and selective PRMT4 inhibitors; however, its high hydrophilicity led to derivatives with poor cellular outcomes. Here, we
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Zhao, Zibo, Emily Jane Rendleman, Aileen Patricia Szczepanski, Marc Alard Morgan, Lu Wang, and Ali Shilatifard. "CARM1-mediated methylation of ASXL2 impairs tumor-suppressive function of MLL3/COMPASS." Science Advances 8, no. 40 (2022). http://dx.doi.org/10.1126/sciadv.add3339.

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An imbalance in the activities of the Polycomb and Trithorax complexes underlies numerous human pathologies, including cancer. The BRCA1 associated protein-1 (BAP1) deubiquitinase negatively regulates Polycomb activity and recruits the Trithorax histone H3K4 methyltransferase, mixed-lineage leukemia protein 3 (MLL3) within Complex Proteins Associated with Set1 (COMPASS), to the enhancers of tumor suppressor genes. We previously demonstrated that the BAP1-MLL3 pathway is mutated in several cancers, yet how BAP1 recruits MLL3 to its target loci remains an important unanswered question. We demons
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Dashti, Parisa, Eric A. Lewallen, Jonathan A. R. Gordon, et al. "Protein arginine methyltransferases PRMT1, PRMT4/CARM1 and PRMT5 have distinct functions in control of osteoblast differentiation." Bone Reports, July 2023, 101704. http://dx.doi.org/10.1016/j.bonr.2023.101704.

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Stouth, Derek W., Alexander Manta, and Vladimir Ljubicic. "Protein Arginine Methyltransferases Exhibit Distinct Cellular Localization and Function During Skeletal Muscle Disuse." FASEB Journal 31, S1 (2017). http://dx.doi.org/10.1096/fasebj.31.1_supplement.1021.3.

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Protein arginine methyltransferase 1 (PRMT1), PRMT4 (also known as co‐activator‐associated arginine methyltransferase 1; CARM1), and PRMT5 catalyze the methylation of arginine residues on target proteins, thereby mediating intracellular processes such as signal transduction and transcriptional control. Although only a few studies have investigated PRMTs in skeletal muscle, evidence strongly suggests that these enzymes regulate skeletal muscle plasticity. However, the function of PRMTs in response to disuse‐induced muscle remodelling remains unknown. Thus, our study objective was to determine w
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Hernando, Carlos E., Sabrina E. Sanchez, Estefanía Mancini, and Marcelo J. Yanovsky. "Genome wide comparative analysis of the effects of PRMT5 and PRMT4/CARM1 arginine methyltransferases on the Arabidopsis thaliana transcriptome." BMC Genomics 16, no. 1 (2015). http://dx.doi.org/10.1186/s12864-015-1399-2.

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Ratovitski, Tamara, Mali Jiang, Robert N. O'Meally, et al. "Interaction of huntingtin with PRMTs and its subsequent arginine methylation affects HTT solubility, phase transition behavior and neuronal toxicity." Human Molecular Genetics, December 9, 2021. http://dx.doi.org/10.1093/hmg/ddab351.

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Abstract Huntington’s disease (HD) is an incurable neurodegenerative disorder caused by a CAG expansion in the huntingtin gene (HTT). Post-translational modifications of huntingtin protein (HTT), such as phosphorylation, acetylation and ubiquitination, have been implicated in HD pathogenesis. Arginine methylation/dimethylation is an important modification with an emerging role in neurodegeneration; however, arginine methylation of HTT remains largely unexplored. Here we report nearly two dozen novel arginine methylation/dimethylation sites on the endogenous HTT from human and mouse brain and h
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Coelho, Fernanda Sales, Sandra Grossi Gava, Luiza Freire Andrade, et al. "Schistosoma mansoni coactivator associated arginine methyltransferase 1 (SmCARM1) effect on parasite reproduction." Frontiers in Microbiology 14 (February 24, 2023). http://dx.doi.org/10.3389/fmicb.2023.1079855.

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IntroductionThe human blood fluke parasite Schistosoma mansoni relies on diverse mechanisms to adapt to its diverse environments and hosts. Epigenetic mechanisms play a central role in gene expression regulation, culminating in such adaptations. Protein arginine methyltransferases (PRMTs) promote posttranslational modifications, modulating the function of histones and non-histone targets. The coactivator-associated arginine methyltransferase 1 (CARM1/PRMT4) is one of the S. mansoni proteins with the PRMT core domain.MethodsWe carried out in silico analyses to verify the expression of SmPRMTs i
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