Human protein arginine methyltransferases in vivo – distinct properties of eight canonical members of the PRMT family

No abstract is available for this paper.

• Publication year

  2009

• Venue

  Journal of Cell Science

• Publication date

  2009-03-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1242/jcs.039933PMID 19208762
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Nucleo‐cytoplasmic shuttling of protein arginine methyltransferase 1 (PRMT1) requires enzymatic activity

  2009cited by this paper
• PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex.

  2008influential reference
• The histone‐binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5

  2008cited by this paper
• Promiscuous Modification of the Nuclear Poly(A)-binding Protein by Multiple Protein-arginine Methyltransferases Does Not Affect the Aggregation Behavior*

  2008cited by this paper
• The protein arginine methyltransferases CARM1 and PRMT1 cooperate in gene regulation

  2008cited by this paper
• Arginine Methylation of the Histone H3 Tail Impedes Effector Binding*

  2008cited by this paper
• PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity.

  2007cited by this paper
• The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing.

  2007cited by this paper
• Regulation of Protein Arginine Methyltransferase 8 (PRMT8) Activity by Its N-terminal Domain*

  2007cited by this paper
• Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1

  2007cited by this paper
• Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms with Distinct Activity, Substrate Specificity, and Subcellular Localization*

  2007cited by this paper
• Ribosomal Protein rpS2 Is Hypomethylated in PRMT3-deficient Mice*

  2007cited by this paper
• Specific regional distribution of protein arginine methyltransferase 8 (PRMT8) in the mouse brain.

  2007cited by this paper
• Arginine methylation at a glance

  2007cited by this paper
• Regulation of flowering time by the protein arginine methyltransferase AtPRMT10

  2007cited by this paper
• PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor.

  2007cited by this paper
• DRE-1: an evolutionarily conserved F box protein that regulates C. elegans developmental age.

  2007cited by this paper
• Multivalent engagement of chromatin modifications by linked binding modules

  2007cited by this paper
• Protein methylation and DNA repair.

  2007cited by this paper
• Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells

  2006cited by this paper
• Histone arginine methylation and its dynamic regulation.

  2006cited by this paper
• Local Chromatin Mobility is Independent of Transcriptional Activity

  2006cited by this paper
• Protein arginine methylation in lymphocyte signaling.

  2006cited by this paper
• Investigating membrane protein dynamics in living cells.

  2006cited by this paper
• FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues.

  2006cited by this paper
• Dynamics of Human Protein Arginine Methyltransferase 1(PRMT1) in Vivo*

  2005cited by this paper
• Arginine methylation an emerging regulator of protein function.

  2005cited by this paper
• PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine*

  2005cited by this paper
• Protein arginine methyltransferases: guardians of the Arg?

  2005cited by this paper
• Arginine Methylation Provides Epigenetic Transcription Memory for Retinoid-Induced Differentiation in Myeloid Cells

  2005cited by this paper
• A Stable Proteinaceous Structure in the Territory of Inactive X Chromosomes*

  2005cited by this paper
• Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver.

  2005cited by this paper
• Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3).

  2005cited by this paper
• PRMT8, a New Membrane-bound Tissue-specific Member of the Protein Arginine Methyltransferase Family*

  2005cited by this paper
• Arginine Methylation of Scaffold Attachment Factor A by Heterogeneous Nuclear Ribonucleoprotein Particle-associated PRMT1*

  2004cited by this paper
• PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits

  2004influential reference
• Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53.

  2004cited by this paper
• Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes.

  2004cited by this paper
• Human Fibrillarin Forms a Sub-complex with Splicing Factor 2-associated p32, Protein Arginine Methyltransferases, and Tubulins α3 and β1 That Is Independent of Its Association with Preribosomal Ribonucleoprotein Complexes*

  2004cited by this paper
• Loss of CARM1 Results in Hypomethylation of Thymocyte Cyclic AMP-regulated Phosphoprotein and Deregulated Early T Cell Development*

  2004cited by this paper
• PRMT7 Is a Member of the Protein Arginine Methyltransferase Family with a Distinct Substrate Specificity*

  2004influential reference
• A methylation-mediator complex in hormone signaling.

  2004cited by this paper
• Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1

  2003cited by this paper
• Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1.

  2003cited by this paper
• Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides.

  2003influential reference
• Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice

  2003cited by this paper
• mSin3A/Histone Deacetylase 2- and PRMT5-Containing Brg1 Complex Is Involved in Transcriptional Repression of the Myc Target Gene cad

  2003cited by this paper
• I. Arginine.

  2002influential reference
• The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity*

  2002cited by this paper
• Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects

  2002cited by this paper
• Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing

  2002cited by this paper
• Protein arginine methyltransferase I: Substrate specificity and role in hnRNP assembly

  2002influential reference
• Identification of Protein Arginine Methyltransferase 2 as a Coactivator for Estrogen Receptor α*

  2002cited by this paper
• PRMT5, Which Forms Distinct Homo-oligomers, Is a Member of the Protein-arginine Methyltransferase Family*

  2001cited by this paper
• PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins*

  2001cited by this paper
• Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy.

  2000influential reference
• Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

  2000influential reference
• Arginine N-Methyltransferase 1 Is Required for Early Postimplantation Mouse Development, but Cells Deficient in the Enzyme Are Viable

  2000cited by this paper
• Regulation of transcription by a protein methyltransferase.

  1999cited by this paper
• Unusual Sites of Arginine Methylation in Poly(A)-binding Protein II and in Vitro Methylation by Protein Arginine Methyltransferases PRMT1 and PRMT3*

  1999cited by this paper
• The Human Homologue of the Yeast Proteins Skb1 and Hsl7p Interacts with Jak Kinases and Contains Protein Methyltransferase Activity*

  1999cited by this paper
• Arginine methylation facilitates the nuclear export of hnRNP proteins.

  1998influential reference
• PRMT 3, a Type I Protein Arginine N-Methyltransferase That Differs from PRMT1 in Its Oligomerization, Subcellular Localization, Substrate Specificity, and Regulation*

  1998influential reference
• Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene

  1997cited by this paper
• The Mammalian Immediate-early TIS21 Protein and the Leukemia-associated BTG1 Protein Interact with a Protein-arginine N-Methyltransferase*

  1996cited by this paper
• A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine.

  1995cited by this paper
• Mobility measurement by analysis of fluorescence photobleaching recovery kinetics.

  1976cited by this paper

• Protein Arginine Methyltransferases in γ-Globin Regulation and Sickle Cell Disease: Emerging Connections to Oxidative Stress

  2026cites this paper
• Biomedical effects of protein arginine methyltransferase inhibitors

  2025cites this paper
• The Identification of a Sub-Micromolar Peptide-Based Protein Arginine Methyltransferase 1 (PRMT1) Inhibitor from a Plate-Based Screening Assay

  2025cites this paper
• Towards the Targeted Protein Degradation of PRMT1

  2024cites this paper
• Oligomerization of protein arginine methyltransferase 1 and its effect on methyltransferase activity and substrate specificity

  2024cites this paper
• Biochemical Properties of CARM1: Impact on Western Blotting and Proteomic Studies

  2024cites this paper
• Methylation and phosphorylation of formin homology domain proteins (Fhod1 and Fhod3) by protein arginine methyltransferase 7 (PRMT7) and Rho kinase (ROCK1)

  2024cites this paper
• Hetero-oligomeric interaction as a new regulatory mechanism for protein arginine methyltransferases.

  2024cites this paper
• Oligomerization of protein arginine methyltransferase 1 and its functional impact on substrate arginine methylation

  2024cites this paper
• The arginine methyltransferase PRMT5 promotes mucosal defense in the intestine

  2023cites this paper
• Protein arginine N-methyltransferase 2 plays a noncatalytic role in the histone methylation activity of PRMT1

  2023cites this paper
• Integrative Evaluation of the Clinical Significance Underlying Protein Arginine Methyltransferases in Hepatocellular Carcinoma

  2023cites this paper
• PRMT5 is a therapeutic target in choroidal neovascularization

  2022cites this paper
• MeCP2 heterochromatin organization is modulated by arginine methylation and serine phosphorylation

  2022cites this paper
• Structure-activity relationship study of a series of nucleoside derivatives bearing sulfonamide scaffold as potent and selective PRMT5 inhibitors.

  2022cites this paper
• Coactivator‐associated arginine methyltransferase 1 controls oligodendrocyte differentiation in the corpus callosum during early brain development

  2022cites this paper
• PRMT1 suppresses doxorubicin-induced cardiotoxicity by inhibiting endoplasmic reticulum stress.

  2022cites this paper
• A peptoid-based inhibitor of protein arginine methyltransferase 1 (PRMT1) induces apoptosis and autophagy in cancer cells

  2022cites this paper
• Impact of posttranslational modifications in pancreatic carcinogenesis and treatments

  2021cites this paper
• Localization of METTL16 at the Nuclear Periphery and the Nucleolus Is Cell Cycle-Specific and METTL16 Interacts with Several Nucleolar Proteins

  2021cites this paper
• A Comprehensive Analysis of the Role of hnRNP A1 Function and Dysfunction in the Pathogenesis of Neurodegenerative Disease

  2021cites this paper
• Malic enzyme 2 connects the Krebs cycle intermediate fumarate to mitochondrial biogenesis.

  2021cites this paper
• Global analysis of protein arginine methylation

  2021cites this paper
• Non-Histone Arginine Methylation by Protein Arginine Methyltransferases.

  2020cites this paper
• Assaying epigenome functions of PRMTs and their substrates.

  2020cites this paper
• Peptidic transition state analogues as PRMT inhibitors.

  2020cites this paper
• PRMT7 regulates RNA-binding capacity and protein stability in Leishmania parasites

  2020cites this paper
• PRMT7 deficiency causes dysregulation of the HCN channels in the CA1 pyramidal cells and impairment of social behaviors

  2020cites this paper
• Glutathionylation Decreases Methyltransferase Activity of PRMT5 and Inhibits Cell Proliferation

  2020cites this paper
• Histone H4-based peptoids are inhibitors of Protein Arginine Methyltransferase 1 (PRMT1).

  2020cites this paper
• PRMT7 methylates eukaryotic translation initiation factor 2α and regulates its role in stress granule formation

  2019cites this paper
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  2019cites this paper
• Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials

  2019cites this paper
• Chemical Probes for Protein Arginine Methyltransferases.

  2019cites this paper
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  2019cites this paper
• Protein arginine methyltransferase biology in humans during acute and chronic skeletal muscle plasticity.

  2019cites this paper
• A patent review of arginine methyltransferase inhibitors (2010–2018)

  2019cites this paper
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  2019cites this paper
• The N-terminal sequence of murine PRMT5 variant 2 is required for Hsp70 interaction and CHIP ligase-mediated degradation.

  2019cites this paper
• A comparative analysis of histone methyltransferases and demethylases in insect genome: A meta-analysis

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• Evaluation of kinetic data: What the numbers tell us about PRMTs.

  2019cites this paper
• Type I Protein Arginine Methyltransferases Overexpression Promotes Transformation and Potentiates Her2/Neu-Driven Tumorigenesis.

  2019cites this paper
• PRMT7 as a unique member of the protein arginine methyltransferase family: A review.

  2019influential citation
• The development and characterization of a chemical probe targeting PRMT1 over PRMT5.

  2019cites this paper
• Novel alternative splice variants of the human protein arginine methyltransferase 1 (PRMT1) gene, discovered using next-generation sequencing.

  2019cites this paper
• Protein arginine N-methyltransferase 2 reverses tamoxifen resistance in breast cancer cells through suppression of ER-α36

  2018cites this paper
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  2018cites this paper
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• A novel splicing isoform of protein arginine methyltransferase 1 (PRMT1) that lacks the dimerization arm and correlates with cellular malignancy

  2018cites this paper
• Identification of Selective, Cell Active Inhibitors of Protein Arginine Methyltransferase 5 through Structure-Based Virtual Screening and Biological Assays

  2018cites this paper
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  2018cites this paper
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  2017cites this paper
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• Comparative Monomethylarginine Proteomics Suggests that Protein Arginine Methyltransferase 1 (PRMT1) is a Significant Contributor to Arginine Monomethylation in Toxoplasma gondii

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  2017cites this paper
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  2016cites this paper
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  2015cites this paper
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  2015cites this paper
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  2015cites this paper
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  2015cites this paper
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  2015cites this paper
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• Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.

  2014cites this paper
• High-glucose-induced CARM1 expression regulates apoptosis of human retinal pigment epithelial cells via histone 3 arginine 17 dimethylation: role in diabetic retinopathy.

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