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PRMT T cell

Wei-Chih Tsai, Sitaram Gayatri, Lucas C Reineke, Gianluca Sbardella, Mark T Bedford, Richard E Lloyd
Stress granules (SGs) are cytoplasmic condensates of stalled messenger ribonucleoprotein complexes (mRNPs) that form when eukaryotic cells encounter environmental stress. RNA binding proteins are enriched for arginine methylation and facilitate SG assembly through interactions involving regions of low amino acid complexity. How methylation of specific RNA binding proteins regulates RNA granule assembly has not been characterized. Here, we examined the potent SG nucleating protein Ras-GAP SH3 Binding Protein 1 (G3BP1), and found that G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain...
September 6, 2016: Journal of Biological Chemistry
Ji Hye Kim, Byong Chul Yoo, Woo Seok Yang, Eunji Kim, Sungyoul Hong, Jae Youl Cho
Protein arginine methyltransferases (PRMTs) mediate the methylation of a number of protein substrates of arginine residues and serve critical functions in many cellular responses, including cancer development, progression, and aggressiveness, T-lymphocyte activation, and hepatic gluconeogenesis. There are nine members of the PRMT family, which are divided into 4 types (types I-IV). Although most PRMTs do not require posttranslational modification (PTM) to be activated, fine-tuning modifications, such as interactions between cofactor proteins, subcellular compartmentalization, and regulation of RNA, via micro-RNAs, seem to be required...
2016: Mediators of Inflammation
Kamal El Bissati, Elena S Suvorova, Hui Xiao, Olivier Lucas, Rajendra Upadhya, Yanfen Ma, Ruth Hogue Angeletti, Michael W White, Louis M Weiss, Kami Kim
UNLABELLED: The arginine methyltransferase family (PRMT) has been implicated in a variety of cellular processes, including signal transduction, epigenetic regulation, and DNA repair pathways. PRMT1 is thought to be responsible for the majority of PRMT activity in Toxoplasma gondii, but its exact function is unknown. To further define the biological function of the PRMT family, we generated T. gondii mutants lacking PRMT1 (Δprmt1) by deletion of the PRMT1 gene. Δprmt1 parasites exhibit morphological defects during cell division and grow slowly, and this phenotype reverses in the Δprmt::PRMT1mRFP complemented strain...
2016: MBio
Neah Likhite, Christopher A Jackson, Mao-Shih Liang, Michelle C Krzyzanowski, Pedro Lei, Jordan F Wood, Barbara Birkaya, Kerry L Michaels, Stelios T Andreadis, Stewart D Clark, Michael C Yu, Denise M Ferkey
Protein arginine methylation regulates diverse functions of eukaryotic cells, including gene expression, the DNA damage response, and circadian rhythms. We showed that arginine residues within the third intracellular loop of the human D2 dopamine receptor, which are conserved in the DOP-3 receptor in the nematode Caenorhabditis elegans, were methylated by protein arginine methyltransferase 5 (PRMT5). By mutating these arginine residues, we further showed that their methylation enhanced the D2 receptor-mediated inhibition of cyclic adenosine monophosphate (cAMP) signaling in cultured human embryonic kidney (HEK) 293T cells...
November 10, 2015: Science Signaling
Masao Maeda, Hitoki Hasegawa, Mai Sugiyama, Toshinori Hyodo, Satoko Ito, Dan Chen, Eri Asano, Akio Masuda, Yoshinori Hasegawa, Michinari Hamaguchi, Takeshi Senga
Proper bioriented attachment of microtubules and kinetochores is essential for the precise distribution of duplicated chromosomes to each daughter cell. An aberrant kinetochore-microtubule attachment results in chromosome instability, which leads to cellular transformation or apoptosis. In this article, we show that ubiquitin-associated protein 2-like (UBAP2L) is necessary for correct kinetochore-microtubule attachment. Depletion of UBAP2L inhibited chromosome alignment in metaphase and delayed progression to anaphase by activating spindle assembly checkpoint signaling...
January 2016: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
Shinsuke Mizutani, Tatsushi Yoshida, Xinyang Zhao, Stephen D Nimer, Masafumi Taniwaki, Tsukasa Okuda
RUNX1 (previously termed AML1) is a frequent target of human leukaemia-associated gene aberrations, and it encodes the DNA-binding subunit of the Core-Binding Factor transcription factor complex. RUNX1 expression is essential for the initiation of definitive haematopoiesis, for steady-state thrombopoiesis, and for normal lymphocytes development. Recent studies revealed that protein arginine methyltransferase 1 (PRMT1), which accounts for the majority of the type I PRMT activity in cells, methylates two arginine residues in RUNX1 (R206 and R210), and these modifications inhibit corepressor-binding to RUNX1 thereby enhancing its transcriptional activity...
September 2015: British Journal of Haematology
Lapo Alinari, Kiran V Mahasenan, Fengting Yan, Vrajesh Karkhanis, Ji-Hyun Chung, Emily M Smith, Carl Quinion, Porsha L Smith, Lisa Kim, John T Patton, Rosa Lapalombella, Bo Yu, Yun Wu, Satavisha Roy, Alessandra De Leo, Stefano Pileri, Claudio Agostinelli, Leona Ayers, James E Bradner, Selina Chen-Kiang, Olivier Elemento, Tasneem Motiwala, Sarmila Majumder, John C Byrd, Samson Jacob, Said Sif, Chenglong Li, Robert A Baiocchi
Epigenetic events that are essential drivers of lymphocyte transformation remain incompletely characterized. We used models of Epstein-Barr virus (EBV)-induced B-cell transformation to document the relevance of protein arginine methyltransferase 5 (PRMT5) to regulation of epigenetic-repressive marks during lymphomagenesis. EBV(+) lymphomas and transformed cell lines exhibited abundant expression of PRMT5, a type II PRMT enzyme that promotes transcriptional silencing of target genes by methylating arginine residues on histone tails...
April 16, 2015: Blood
Kaylen Lott, Lu Zhu, John C Fisk, Danielle L Tomasello, Laurie K Read
Arginine methylation is a common posttranslational modification that has far-reaching cellular effects. Trypanosoma brucei is an early-branching eukaryote with four characterized protein arginine methyltransferases (PRMTs), one additional putative PRMT, and over 800 arginine methylated proteins, suggesting that arginine methylation has widespread impacts in this organism. While much is known about the activities of individual T. brucei PRMTs (TbPRMTs), little is known regarding how TbPRMTs function together in vivo...
October 2014: MicrobiologyOpen
Michel Pelletier, Alyssa S Frainier, Dominic N Munini, Jenna M Wiemer, Amber R Karpie, Jeff J Sattora
BACKGROUND: Arginine methylation is a post-translational modification that expands the functional diversity of proteins. Kinetoplastid parasites contain a relatively large group of protein arginine methyltransferases (PRMTs) compared to other single celled eukaryotes. Several T. brucei proteins have been shown to serve as TbPRMT substrates in vitro, and a great number of proteins likely to undergo methylation are predicted by the T. brucei genome. This indicates that a large number of proteins whose functions are modulated by arginine methylation await discovery in trypanosomes...
2013: BMC Microbiology
Shaun E Hunter, Emily F Finnegan, Dimitrios G Zisoulis, Michael T Lovci, Katya V Melnik-Martinez, Gene W Yeo, Amy E Pasquinelli
The let-7 microRNA (miRNA) regulates cellular differentiation across many animal species. Loss of let-7 activity causes abnormal development in Caenorhabditis elegans and unchecked cellular proliferation in human cells, which contributes to tumorigenesis. These defects are due to improper expression of protein-coding genes normally under let-7 regulation. While some direct targets of let-7 have been identified, the genome-wide effect of let-7 insufficiency in a developing animal has not been fully investigated...
2013: PLoS Genetics
Donghang Cheng, Vidyasiri Vemulapalli, Mark T Bedford
Arginine methylation was discovered in the mid-1960s. About 15 years ago, the first protein arginine N-methyltransferase (PRMT) enzyme was described. The PRMT family now stands at nine members, and these enzymes play a key role in regulating a multitude of cellular events. The majority of the PRMTs have been deleted in mice, thus providing genetically tractable systems for in vivo and cell-based studies. These studies have implicated this posttranslational modification in chromatin remodeling, transcriptional regulation, RNA processing, protein/RNA trafficking, signal transduction, and DNA repair...
2012: Methods in Enzymology
Elisabeth-Maria Bissinger, Ralf Heinke, Astrid Spannhoff, Adrien Eberlin, Eric Metzger, Vincent Cura, Pierre Hassenboehler, Jean Cavarelli, Roland Schüle, Mark T Bedford, Wolfgang Sippl, Manfred Jung
Arginine methylation is an epigenetic modification that receives increasing interest as it plays an important role in several diseases. This is especially true for hormone-dependent cancer, seeing that histone methylation by arginine methyltransferase I (PRMT1) is involved in the activation of sexual hormone receptors. Therefore, PRMT inhibitors are potential drugs and interesting tools for cell biology. A dapsone derivative called allantodapsone previously identified by our group served as a lead structure for inhibitor synthesis...
June 15, 2011: Bioorganic & Medicinal Chemistry
Donghang Cheng, Mark T Bedford
Arginine methylation is a common post-translational modification that has been strongly implicated in transcriptional regulation. The arginine methyltransferases (PRMTs) were first reported as transcriptional coactivators for the estrogen and androgen receptors. Compounds that inhibit these enzymes will provide us with valuable tools for dissecting the roles of these enzymes in cells, and will possibly also have therapeutic applications. In order to identify such inhibitors of the PRMTs, we have previously performed a high-throughput screen using a small molecule library...
January 24, 2011: Chembiochem: a European Journal of Chemical Biology
John C Fisk, Cecilia Zurita-Lopez, Joyce Sayegh, Danielle L Tomasello, Steven G Clarke, Laurie K Read
Arginine methylation is a widespread posttranslational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). In Saccharomyces cerevisiae and mammals, this modification affects multiple cellular processes, such as chromatin remodeling leading to transcriptional regulation, RNA processing, DNA repair, and cell signaling. The protozoan parasite Trypanosoma brucei possesses five putative PRMTs in its genome. This is a large number of PRMTs relative to other unicellular eukaryotes, suggesting an important role for arginine methylation in trypanosomes...
June 2010: Eukaryotic Cell
Kevin Bonham, Saskia Hemmers, Yeon-Hee Lim, Dawn M Hill, M G Finn, Kerri A Mowen
The protein arginine methyltransferase (PRMT) family of enzymes catalyzes the transfer of methyl groups from S-adenosylmethionine to the guanidino nitrogen atom of peptidylarginine to form monomethylarginine or dimethylarginine. We created several less polar analogs of the specific PRMT inhibitor arginine methylation inhibitor-1, and one such compound was found to have improved PRMT inhibitory activity over the parent molecule. The newly identified PRMT inhibitor modulated T-helper-cell function and thus may serve as a lead for further inhibitors useful for the treatment of immune-mediated disease...
May 2010: FEBS Journal
Richard V Parry, Stephen G Ward
Protein arginine methylation has emerged as a key regulator of signal transduction with an important role in T lymphocyte activation. The predominant methyl transferase PRMT-1 is highly expressed in T helper cells, and ligation of the T cell antigen and costimulatory receptors, induces arginine methylation on several cytoplasmic proteins. Global inhibition of methyl transferases can result in signaling defects in CD4 T cells and profound immunosuppression. Here we suggest that manipulating protein arginine methylation could be a feasible strategy to modulate T lymphocyte function, presenting a novel approach towards immunotherapy and the treatment of T cell-mediated disorders such as autoimmune disease and transplant rejection...
April 2010: Trends in Immunology
A Kousaka, Y Mori, Y Koyama, T Taneda, S Miyata, M Tohyama
Protein arginine N-methyltransferase (PRMT) 8 was first discovered from a database search for genes harboring four conserved methyltransferase motifs, which shares more than 80% homology to PRMT1 in amino acid [Lee J, Sayegh J, Daniel J, Clarke S, Bedford MT (2005) PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem 280:32890-32896]. Interestingly, its tissue distribution is strikingly restricted to mouse CNS. To characterize the function in the CNS neurons, we raised an antiserum against PRMT8 to perform immunohistochemistry (IHC) and Western blot analysis...
November 10, 2009: Neuroscience
John C Fisk, Joyce Sayegh, Cecilia Zurita-Lopez, Sarita Menon, Vladimir Presnyak, Steven G Clarke, Laurie K Read
Arginine methylation is a widespread post-translational modification of proteins catalyzed by a family of protein arginine methyltransferases (PRMTs). The ancient protozoan parasite, Trypanosoma brucei, possesses five putative PRMTs, a relatively large number for a single-celled eukaryote. Trypanosomatids lack gene regulation at the level of transcription, instead relying on post-transcriptional control mechanisms that act at the levels of RNA turnover, translation, and editing, all processes that likely involve multiple RNA-binding proteins, which are common targets of arginine methylation...
April 24, 2009: Journal of Biological Chemistry
Frank Herrmann, Peter Pably, Carmen Eckerich, Mark T Bedford, Frank O Fackelmayer
Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of protein arginine methyltransferases (PRMTs). Functionally, the modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. All members have been, to different degrees, characterized individually and their implication in cellular processes has been inferred from characterizing substrates and interactions...
March 1, 2009: Journal of Cell Science
Martin Jansson, Stephen T Durant, Er-Chieh Cho, Sharon Sheahan, Mariola Edelmann, Benedikt Kessler, Nicholas B La Thangue
Activation of the p53 tumour suppressor protein in response to DNA damage leads to apoptosis or cell-cycle arrest. Enzymatic modifications are widely believed to affect and regulate p53 activity. We describe here a level of post-translational control that has an important functional consequence on the p53 response. We show that the protein arginine methyltransferase (PRMT) 5, as a co-factor in a DNA damage responsive co-activator complex that interacts with p53, is responsible for methylating p53. Arginine methylation is regulated during the p53 response and affects the target gene specificity of p53...
December 2008: Nature Cell Biology
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