The Methyltransferases PRMT4/CARM1 and PRMT5 Control Differentially Myogenesis in Zebrafish

Batut, Julie; Duboé, Carine; Vandel, Laurence

doi:10.1371/journal.pone.0025427

Cited by 38 publications

(45 citation statements)

References 34 publications

(39 reference statements)

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“…These adaptations depend on the chronic activation or inhibition of various intracellular signaling pathways, which result in altered skeletal muscle gene expression (2,31). Intracellular signaling molecules such as peroxisome proliferator-activated receptor (PPAR)-γ coactivator-1α (PGC-1α), calcineurin (CN), p38 mitogen-activated protein kinase (p38), AMP-activated protein kinase (AMPK), silent mating type information regulator 2 homologue 1 (SIRT1), PPARβ and tumor suppressor protein p53 play a role in remodelling skeletal muscle toward a slower, more oxidative phenotype (16,18,19,20,21,22,23,24,25). In contrast, receptor interacting protein 140 (RIP140), E2F transcription factor 1 (E2F1), nuclear receptor corepressor 1 (NCoR1), and Baf60c have been shown to promote faster, more glycolytic characteristics (26,27,28,29,32).…”

Section: Skeletal Muscle Plasticitymentioning

confidence: 99%

“…enhancer factor-2C (MEF2C) (175,176). In contrast, PRMT5 is required for early gene expression, suggesting that distinct PRMTs are preferentially active at different times throughout myogenesis (134,176,180).…”

Section: The Role Of Protein Arginine Methyltransferases In Skeletal mentioning

confidence: 99%

“…In contrast, PRMT5 is required for early gene expression, suggesting that distinct PRMTs are preferentially active at different times throughout myogenesis (134,176,180). PRMT5 has also been reported to regulate myogenin, MEF2C, MyoD, and myogenic regulatory factor 5 (Myf5) expression (137,176,178,181). In addition, CARM1 and PRMT5 can be Additionally, PRMT1 and CARM1 serve as important regulators of skeletal muscle glucose metabolism (173,174), which is profoundly affected during exercise.…”

Section: The Role Of Protein Arginine Methyltransferases In Skeletal mentioning

confidence: 99%

“…PRMT1, CARM1, and PRMT5 are emerging players in skeletal muscle biology (20,23,24,25,31). We found that PRMT gene expression at the mRNA and protein levels was increased before and during skeletal muscle atrophy.…”

Section: Muscle Disuse Elicits Alterations In Prmt Content Localizatmentioning

confidence: 99%

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Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity

Stouth

Manta

Ljubicic

2018

American Journal of Physiology-Cell Physiology

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Lay AbstractSkeletal muscle is a plastic tissue that is capable of adapting to various physiological demands. Previous work suggests that protein arginine methyltransferases (PRMTs) are important players in the regulation of skeletal muscle remodelling. However, their role in disuse-induced muscle plasticity is unknown. Therefore, the purpose of this study was to investigate the role of PRMTs within the context of early, upstream signaling pathways that mediate disuse-evoked muscle remodelling. We found differential responses of the PRMTs to muscle denervation, suggesting a unique sensitivity to, or regulation by, potential upstream signaling pathways. AMP-activated protein kinase (AMPK) was among the molecules that experienced a rapid change in activity following disuse. These alterations in AMPK predicted many of the modifications in PRMT biology during inactivity, suggesting that PRMTs factor into the molecular mechanisms that precede neurogenic muscle atrophy. This study expands our understanding of the role of PRMTs in regulating skeletal muscle plasticity.

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Section: Skeletal Muscle Plasticitymentioning

confidence: 99%

Section: The Role Of Protein Arginine Methyltransferases In Skeletal mentioning

confidence: 99%

Section: The Role Of Protein Arginine Methyltransferases In Skeletal mentioning

confidence: 99%

Section: Muscle Disuse Elicits Alterations In Prmt Content Localizatmentioning

confidence: 99%

See 2 more Smart Citations

Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity

Stouth

Manta

Ljubicic

2018

American Journal of Physiology-Cell Physiology

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“…These results raise the possibility that CREBBP methylation may play an important role in the regulation of CREBBP function during embryonic development. Of note, we have previously shown that carm1 is dynamically expressed during zebrafish development and that CARM1 controls myogenesis in vivo (Batut et al, 2011). However, whether and where CREBBP and in particular its methylated forms are expressed during vertebrate development remain unexplored.…”

mentioning

confidence: 99%

Expression patterns of CREB binding protein (CREBBP) and its methylated species during zebrafish development

Batut¹,

Duboé²,

Vandel³

2015

Int. J. Dev. Biol.

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Proper embryonic development requires a fine-tuned control of gene expression, which is achieved in part through the activity of transcription coactivators or corepressors. The nuclear coactivator cAMP-response element-binding protein (CREB) binding protein (CREBBP or CBP) interacts with numerous transcription factors and thereby plays a key role in various signaling pathways. Interestingly, in cell-based studies CREBBP activity is modulated by post-translational modifications such as methylation on arginine residues which is catalyzed by coactivator-associated arginine methyltransferase 1 (CARM1). However, whether and where CREBBP, and in particular its methylated forms, are expressed during development in vertebrates has not been addressed so far. Here, we analyzed the expression of the two crebbp genes (crebbpa & crebbpb) during zebrafish development using both RT-qPCR and in situ hybridization. We found that while crebbpa expression is higher in posterior, caudal nascent somites during somitogenesis, crebbpb accumulates in anterior, rostral, and more mature somites. In addition, crebbpa mRNA is enriched in the central myotome at 24 hpf indicating that its expression is spatially and temporally controlled. We next characterized the expression of CREBBP protein from blastula to gastrula stages by immunohistochemistry. We found that while CREBBP is clearly cytoplasmic in the early blastula, it becomes both cytoplasmic and nuclear at 30% epiboly before turning mainly nuclear during gastrulation. Of interest, CREBBP methylated species appear to be mainly nuclear from 30% epiboly to 6-somite stage. This suggests that methylation may regulate CREBBP import to the nucleus during zebrafish development and could therefore participate in the control of early developmental processes.

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Identification, expression and functional analysis of prmt7 in medaka Oryzias latipes

Zhu

Hou

et al. 2020

J Exp Zool Pt B

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Arginine methylation is an important posttranslational modification and catalyzed by a family of protein arginine methyltransferases (PRMTs). PRMT7 is the type III PRMT and produces solely monomethylarginine products. PRMT7 has been found to play important roles in multiple biological processes in mammals. However, the expression pattern and function of Prmt7 remain largely unknown in fish. In this study, we characterized the medaka prmt7 gene and determined its expression pattern and function during embryogenesis and germ cell development. The results showed that the chromosomal location and gene structure of medaka prmt7 were similar to its mammalian orthologs. Comparisons of deduced amino acid sequences indicated that medaka Prmt7 was a homolog of human PRMT7 with two methyltransferase domains. Reverse transcription‐polymerase chain reaction (RT‐PCR) and real time RT‐PCR revealed that medaka prmt7 had maternal origin with continuous and dynamical expression during embryonic development. Whole‐mount in situ hybridization analysis observed that the transcripts of prmt7 were ubiquitous at morula and gastrula stage, and were later riched in the brain and otic vesicles during embryogenesis. In the adult stage, prmt7 messenger RNA was detected in all examined tissues with the high levels in the ovary and testis. The expression of prmt7 in the gonads was restricted to oocytes of the ovary and spermatids/sperm of the testis. Functional analysis showed that knockdown of medaka prmt7 did not reduce the total number of primordial germ cells (PGCs) in vivo but significantly affected PGCs distribution during embryonic development. These results indicate that prmt7 may be involved in germ cell development in medaka.

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The Methyltransferases PRMT4/CARM1 and PRMT5 Control Differentially Myogenesis in Zebrafish

Cited by 38 publications

References 34 publications

Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity

Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity

Expression patterns of CREB binding protein (CREBBP) and its methylated species during zebrafish development

Identification, expression and functional analysis of prmt7 in medaka Oryzias latipes

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