Protein Arginine Methyltransferase 5 (PRMT5) Signaling Suppresses Protein Kinase Cδ- and p38δ-dependent Signaling and Keratinocyte Differentiation

Kanade, Santosh R.; Eckert, Richard L.

doi:10.1074/jbc.m111.331660

Cited by 24 publications

(32 citation statements)

References 64 publications

(101 reference statements)

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“…We further showed that PRMT5 acts to enhance cell survival by catalyzing symmetric dimethyl arginine modification of target proteins in this complex, leading to inhibition of p38␦ activity (20). This represents a mechanism whereby PRMT5 acts to suppress activity in a growth suppression signaling cascade.…”

Section: Discussionmentioning

confidence: 77%

“…Our recent mass spectrometry analysis identified PRMT5, a type II symmetric arginine methyltransferase, as a novel component of the PKC␦/p38␦ regulatory complex (20). We further showed that PRMT5 acts to enhance cell survival by catalyzing symmetric dimethyl arginine modification of target proteins in this complex, leading to inhibition of p38␦ activity (20).…”

Section: Discussionmentioning

confidence: 86%

“…MEP50 Regulation of Cell Proliferation-A previous study showed that PRMT5 acts to enhance keratinocyte survival and proliferation (20). Because MEP50 is frequently engaged as a PRMT5 cofactor required for PRMT5 activation, we examined whether altering MEP50 expression regulates keratinocyte proliferation.…”

Section: Mep50 Distribution In the Epidermis-mep50 Localizes Inmentioning

confidence: 99%

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Methylosome Protein 50 and PKCδ/p38δ Protein Signaling Control Keratinocyte Proliferation via Opposing Effects on p21Cip1 Gene Expression

Saha¹,

Eckert

2015

Journal of Biological Chemistry

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Background: Keratinocytes cease proliferation during differentiation, and the mechanism that mediates these events is not well understood. Results: PRMT5/MEP50 control p21Cip1 promoter methylation to silence gene expression, and this is reversed by PKC␦/p38␦ signaling. Conclusion: PRMT5/MEP50 and PKC␦/p38␦ signaling produce opposing actions to control keratinocyte proliferation during differentiation. Significance: This study describes cross-talk between MAPK signaling and epigenetic mechanisms to control cell proliferation.

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Section: Discussionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 86%

Section: Mep50 Distribution In the Epidermis-mep50 Localizes Inmentioning

confidence: 99%

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Methylosome Protein 50 and PKCδ/p38δ Protein Signaling Control Keratinocyte Proliferation via Opposing Effects on p21Cip1 Gene Expression

Saha¹,

Eckert

2015

Journal of Biological Chemistry

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“…Reciprocal regulation of protein kinase activity by Arg methylation has also been proposed (49). Although we have not identified the PRMT that methylates Nav1.2 in vivo, the likely candidate is PRMT8, a membrane-associated PRMT specifically expressed in the brain (33) where it is found at high levels in neurons (50,51).…”

Section: Discussionmentioning

confidence: 79%

Reciprocal Changes in Phosphorylation and Methylation of Mammalian Brain Sodium Channels in Response to Seizures

Baek

Rubinstein

Scheuer

et al. 2014

Journal of Biological Chemistry

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Background: Sodium channels underlie neuronal excitability and are regulated by seizures. Results: Mass spectrometric analysis of brain sodium channels revealed novel phosphorylation and methylation sites that decreased and increased, respectively, after seizures. Inducing methylation increased sodium channel activity. Conclusion: Reciprocal phosphorylation and methylation after seizures will alter sodium channel function. Significance: Such regulation would impact neuronal excitability.

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“…8B). Previous reports have shown that p38 can be dimethylated at arginine residues, whereby its activity is modulated (49). Thus, we tested whether p38 can be symmetrically methylated by Prmt7 by using an antibody recognizing symmetric dimethylation of arginine (Sym10).…”

Section: Methylation Inhibition Abolishes P38 Activation Induced By Pmentioning

confidence: 99%

Prmt7 Deficiency Causes Reduced Skeletal Muscle Oxidative Metabolism and Age-Related Obesity

et al. 2016

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Maintenance of skeletal muscle function is critical for metabolic health and the disruption of which exacerbates many chronic diseases such as obesity and diabetes. Skeletal muscle responds to exercise or metabolic demands by a fiber-type switch regulated by signaling-transcription networks that remains to be fully defined. Here, we report that protein arginine methyltransferase 7 (Prmt7) is a key regulator for skeletal muscle oxidative metabolism. Prmt7 is expressed at the highest levels in skeletal muscle and decreased in skeletal muscles with age or obesity. Prmt7−/− muscles exhibit decreased oxidative metabolism with decreased expression of genes involved in muscle oxidative metabolism, including PGC-1α. Consistently, Prmt7−/− mice exhibited significantly reduced endurance exercise capacities. Furthermore, Prmt7−/− mice exhibit decreased energy expenditure, which might contribute to the exacerbated age-related obesity of Prmt7−/− mice. Similarly to Prmt7−/− muscles, Prmt7 depletion in myoblasts also reduces PGC-1α expression and PGC-1α–promoter driven reporter activities. Prmt7 regulates PGC-1α expression through interaction with and activation of p38 mitogen-activated protein kinase (p38MAPK), which in turn activates ATF2, an upstream transcriptional activator for PGC-1α. Taken together, Prmt7 is a novel regulator for muscle oxidative metabolism via activation of p38MAPK/ATF2/PGC-1α.

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Protein Arginine Methyltransferase 5 (PRMT5) Signaling Suppresses Protein Kinase Cδ- and p38δ-dependent Signaling and Keratinocyte Differentiation

Cited by 24 publications

References 64 publications

Methylosome Protein 50 and PKCδ/p38δ Protein Signaling Control Keratinocyte Proliferation via Opposing Effects on p21Cip1 Gene Expression

Methylosome Protein 50 and PKCδ/p38δ Protein Signaling Control Keratinocyte Proliferation via Opposing Effects on p21Cip1 Gene Expression

Reciprocal Changes in Phosphorylation and Methylation of Mammalian Brain Sodium Channels in Response to Seizures

Prmt7 Deficiency Causes Reduced Skeletal Muscle Oxidative Metabolism and Age-Related Obesity

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