Arginine Methylation Molecular Cell

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Arginine Methylation Molecular Cell Mark T. Bedford, Stéphane Richard  Molecular Cell  Volume 18, Issue 3, Pages 263-272 (April 2005) DOI: 10.1016/j.molcel.2005.04.003 Copyright © 2005 Elsevier Inc. Terms and Conditions

Figure 1 The Protein Arginine Methyltransferase Family (A) There are currently eight mammalian members of the PRMT family, which harbor signature motifs I; post I, post II, and post III; and the conserved THW loop (in black). PRMT7 has a duplication of these motifs. PRMT2 and PRMT3 have an SH3 domain and a Zn2+ finger, respectively, which likely facilitate substrate recognition. The accession numbers for the PRMTs are as follows: AAF62893 for hPRMT1, AAH00727 for hPRMT2, AAC39837 for hPRMT3, NP_954592 for CARM1, AAF04502 for hPRMT5, Q96LA8 for hPRMT6, NP_061896 for hPRMT7, and DAA01382 for mPRMT8. The number of residues is indicated at the C terminus of the PRMTs. (B) Type I and type II PRMTs generate monomethylarginine. The generation of asymmetric dimethylarginine is catalyzed by type I, and the production of symmetric dimethylarginine is catalyzed by the type II enzymes. Molecular Cell 2005 18, 263-272DOI: (10.1016/j.molcel.2005.04.003) Copyright © 2005 Elsevier Inc. Terms and Conditions

Figure 2 A List of Known PRMT Substrates A large number of additional substrates has been identified using mass spectrometry approaches (Boisvert et al., 2003; Ong et al., 2004; Wu et al., 2004), but in many of these cases the enzyme responsible for the arginine methylation remains unknown. Abbreviations: EWS, Ewing Sarcoma; SAF-A, hnRNPU; CIRP, cold-inducible RNA binding protein; ILF-3, interleukin enhancer binding factor 3; TLS/FUS, Translocated in liposarcoma; ZF5, Zn2+ finger 5; p137GP1, GPI-anchor protein p137; SAMT1, substrate of arginine methyl transferase 1; TARPP, thymocyte cyclic AMP-regulated phosphoprotein. Molecular Cell 2005 18, 263-272DOI: (10.1016/j.molcel.2005.04.003) Copyright © 2005 Elsevier Inc. Terms and Conditions

Figure 3 Cellular Processes Regulated by Arginine Methylation PRMTs have been implicated in a number of basic cellular actions, including RNA processing, transcriptional regulation, signal transduction, and DNA repair. Methylarginines are denoted by a red dot. Molecular Cell 2005 18, 263-272DOI: (10.1016/j.molcel.2005.04.003) Copyright © 2005 Elsevier Inc. Terms and Conditions

Figure 4 Molecular Mechanisms Regulating Arginine Methylation (A) PRMT specificity and/or activity may be influenced by binding proteins. (B) The peptidyl arginine deiminases can block methylation by converting arginine (and MMA) to citrulline. In addition, a family of amine oxidases may be able to demethylate arginine residues in the same fashion as they demethylate lysine residues. Abbreviations: BTG/TIS21, B cell translocation gene/tetradecanoyl phorbol acetate-inducible sequences; DAL-1, differentially expressed in adenocarcinoma of the lung. Molecular Cell 2005 18, 263-272DOI: (10.1016/j.molcel.2005.04.003) Copyright © 2005 Elsevier Inc. Terms and Conditions