Drosophila arginine methyltransferase 1 (DART1) is an ecdysone receptor co-repressor

Kimura, Shuhei; Sawatsubashi, Shun; S, Itó; Kouzmenko, Alexander; Suzuki, Eriko; Zhao, Yue; Yamagata, Kazuya; Tanabe, Masahiko; Ueda, Takashi; Fujiyama, Sari; Murata, Takuya; Matsukawa, Hiroyuki; Takeyama, Ken Ichi; Yaegashi, Nobuo; Kato, Shigeaki

doi:10.1016/j.bbrc.2008.05.003

Cited by 36 publications

(21 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Many types of histone modifiers are involved in ecdysone-mediated gene transcription in D. melanogaster : the acetyltransferases p160/SRC/Taiman (6) and p300/CBP (60), the lysine methyltransferase TRR (111), the poly(ADP-ribose) polymerase PARP (109, 131), and the arginine methyltransferase DART1 (58). All these histone modifiers interact with EcR in a ligand-dependent manner, thereby working as coactivators (except DART1, which is a corepressor) of ecdysone signaling.…”

Section: Molecular Basis Of Stage- and Tissue-specific Responses To Ementioning

confidence: 99%

Ecdysone Control of Developmental Transitions: Lessons from Drosophila Research

Yamanaka

Rewitz

O’Connor

2013

Annu. Rev. Entomol.

572

517

View full text Add to dashboard Cite

The steroid hormone ecdysone is the central regulator of insect developmental transitions. Recent new advances in our understanding of ecdysone action have relied heavily on the application of Drosophila melanogaster molecular genetic tools to study insect metamorphosis. In this review, we focus on three major aspects of Drosophila ecdysone biology: (a) factors that regulate the timing of ecdysone release, (b) molecular basis of stage- and tissue-specific responses to ecdysone, and (c) feedback regulation and coordination of ecdysone signaling.

show abstract

Section: Molecular Basis Of Stage- and Tissue-specific Responses To Ementioning

confidence: 99%

Ecdysone Control of Developmental Transitions: Lessons from Drosophila Research

Yamanaka

Rewitz

O’Connor

2013

Annu. Rev. Entomol.

572

517

View full text Add to dashboard Cite

show abstract

“…JIL-1 is involved in early elongation of a broad range of genes, and is considered as a hallmark of early transcription elongation in Drosophila [65]. A Drosophila arginine methyltransferase1 (DART1) acts as a co-repressor of EcR [66], and the expression of FTZ-F1 is controlled by the corepressor B lymphocyte-induced maturation protein 1 (dBlimp-1) [67]. b-catenin reduces basal and hormone-induced transcriptional activity of all ecdysone receptor isoforms (Ruff, unpublished observation).…”

Section: Influence Of Comodulatorsmentioning

confidence: 99%

Ecdysteroid hormone action

Spindler

Honl

Tremmel

et al. 2009

Cell. Mol. Life Sci.

104

View full text Add to dashboard Cite

Several reviews devoted to various aspects of ecdysone research have been published during the last few years. Therefore, this article concentrates mainly on the considerable progress in ecdysone research observed recently, and will cover the results obtained during the last 2 years. The main emphasis is put on the molecular mode of ecdysteroid receptor-mediated hormone action. Two examples of interaction with other hormonal signalling pathways are described, namely crosstalk with juvenile hormone and insulin. Some selected, recently investigated examples of the multitude of hormonal responses are described. Finally, ecological aspects and some practical applications are discussed.

show abstract

“…To further explore the physiological roles of asymmetric arginine dimethylation, we attempted to system-atically identify in vivo substrates of PRMT-1. As we reported previously (9), nematode C. elegans PRMT-1 is the predominant type I arginine methyltransferase, and the prmt-1(ok2710) null mutant is viable, unlike lethal phenotypes of PRMT-1-deficient mouse and Drosophila (7,8). We therefore employed C. elegans as an ideal animal model for screening in vivo substrates of PRMT-1 with the strategy of a two-dimensional (2-D) proteomic analysis (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…A family of protein arginine methyltransferases (PRMT) is responsible for catalyzing first the formation of an MMA as an intermediate, and subsequently type I enzymes, including PRMT-1, -2, -3, -4, -6, and -8, further catalyze the generation of ADMA, while type II enzymes, including PRMT-5, PRMT-7, and FBXO11, catalyze the generation of SDMA (5). Among them, PRMT-1 is known to be the predominant type I enzyme in mammalian cells, whereas its physiological significance at the whole-body level has remained unclear due to embryonic lethality in the null mutants of mouse and Drosophila (6)(7)(8). Meanwhile, we have previously reported that the loss-of-function mutants of nematode PRMT-1 in Caenorhabditis elegans are viable (9).…”

mentioning

confidence: 99%

Asymmetric Arginine Dimethylation Modulates Mitochondrial Energy Metabolism and Homeostasis in Caenorhabditis elegans

Luo

Daitoku

Araoi

et al. 2017

Molecular and Cellular Biology

View full text Add to dashboard Cite

Protein arginine methyltransferase 1 (PRMT-1) catalyzes asymmetric arginine dimethylation on cellular proteins and modulates various aspects of biological processes, such as signal transduction, DNA repair, and transcriptional regulation. We have previously reported that the null mutant of prmt-1 in Caenorhabditis elegans exhibits a slightly shortened life span, but the physiological significance of PRMT-1 remains largely unclear. Here we explored the role of PRMT-1 in mitochondrial function as hinted by a two-dimensional Western blot-based proteomic study. Subcellular fractionation followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis showed that PRMT-1 is almost entirely responsible for asymmetric arginine dimethylation on mitochondrial proteins. Importantly, isolated mitochondria from prmt-1 mutants represent compromised ATP synthesis in vitro, and wholeworm respiration in prmt-1 mutants is decreased in vivo. Transgenic rescue experiments demonstrate that PRMT-1-dependent asymmetric arginine dimethylation is required to prevent mitochondrial reactive oxygen species (ROS) production, which consequently causes the activation of the mitochondrial unfolded-protein response. Furthermore, the loss of enzymatic activity of prmt-1 induces food avoidance behavior due to mitochondrial dysfunction, but treatment with the antioxidant N-acetylcysteine significantly ameliorates this phenotype. These findings add a new layer of complexity to the posttranslational regulation of mitochondrial function and provide clues for understanding the physiological roles of PRMT-1 in multicellular organisms. KEYWORDS Caenorhabditis elegans, PRMT-1, asymmetric arginine methylation, mitochondriaA rginine methylation has drawn attention as a widespread posttranslational modification that often occurs in RNA-binding proteins, signaling molecules, DNA repair machinery, and transcriptional factors (1-5). This modification is classified according to the number and position of the methyl groups on a guanidino nitrogen of arginine residue, namely, monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), or symmetric dimethylarginine (SDMA). A family of protein arginine methyltransferases (PRMT) is responsible for catalyzing first the formation of an MMA as an intermediate, and subsequently type I enzymes, including further catalyze the generation of ADMA, while type II enzymes, including PRMT-5, PRMT-7, and FBXO11, catalyze the generation of SDMA (5). Among them, PRMT-1 is known to be the predominant type I enzyme in mammalian cells, whereas its physiological significance at the whole-body level has remained unclear due to embryonic

show abstract

Drosophila arginine methyltransferase 1 (DART1) is an ecdysone receptor co-repressor

Cited by 36 publications

References 34 publications

Ecdysone Control of Developmental Transitions: Lessons from Drosophila Research

Ecdysone Control of Developmental Transitions: Lessons from Drosophila Research

Ecdysteroid hormone action

Asymmetric Arginine Dimethylation Modulates Mitochondrial Energy Metabolism and Homeostasis in Caenorhabditis elegans

Contact Info

Product

Resources

About