Histone H3 as a novel substrate for MAP kinase phosphatase-1

Kinney, Corttrell M.; Chandrasekharan, Unni M.; Yang, Lin; Shen, Jianzhong; Kinter, Michael; McDermott, Michael S.; DiCorleto, Paul E.

doi:10.1152/ajpcell.00492.2008

Cited by 39 publications

(32 citation statements)

References 60 publications

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“…These findings are in agreement with another study in keratinocytes, showing that DMF inhibited MSK-1 phosphorylation at Ser376 independently of p38 or ERK MAPK [21]. MKP-1, an endogenous inhibitor of MAPK, can be upregulated by reduced GSH levels [29] and, besides inhibiting MAPK p38 and ERK in ASMCs [23], it was reported to dephosphorylate histone H3 at Ser10 [30]. However, DMF treatment did not affect MKP-1 level in our study, suggesting that it does not mediate the inhibitory effect of DMF on histone H3 phosphorylation.…”

Section: Discussionsupporting

confidence: 91%

IκBα glutathionylation and reduced histone H3 phosphorylation inhibit eotaxin and RANTES

Seidel

Roth

et al. 2011

Eur Respir J

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Airway smooth muscle cells (ASMCs) secrete eotaxin and RANTES (regulated on activation, normal T-cell expressed and secreted) in response to tumour necrosis factor (TNF)-a, which is inhibited by the nuclear factor (NF)-kB inhibitor dimethylfumarate (DMF). NF-kB/IkB (inhibitor of NF-kB) glutathionylation and changes in chromatin remodelling can inhibit NF-kB activity. In this study, we determined whether NF-kB/IkB glutathionylation and reduced histone H3 phosphorylation might underlie the inhibitory effect of DMF on NF-kB activity, and eotaxin and RANTES secretion.Primary human ASMCs were treated with DMF, diamide and/or glutathione (GSH) ethylester (OEt) prior to TNF-a stimulation and were subsequently analysed by ELISA, electrophoretic mobility shift assay, immunofluorescence, co-immunoprecipitation or immunoblotting.DMF reduced intracellular GSH and induced IkBa glutathionylation (IkBa-SSG), which inhibited IkBa degradation, NF-kB p65 nuclear entry and NF-kB/DNA binding. In addition, DMF inhibited the phosphorylation of histone H3, which was possibly mediated by the inhibitory effect of DMF on mitogen-and stress-activated protein kinase (MSK)-1. However, p38 mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase MAPK and MAPK phosphatase-1, upstream of MSK-1, were not inhibited by DMF. Importantly, DMF-mediated effects on NF-kB, histone H3, eotaxin and RANTES were reversed by addition of GSH-OEt.Our data suggest that DMF inhibits NF-kB-dependent eotaxin and RANTES secretion by reduction of GSH with subsequent induction of IkBa-SSG and inhibition of histone H3 phosphorylation. Our findings offer new potential drug targets to reduce airway inflammation in asthma.

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Section: Discussionsupporting

confidence: 91%

IκBα glutathionylation and reduced histone H3 phosphorylation inhibit eotaxin and RANTES

Seidel

Roth

et al. 2011

Eur Respir J

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“…9C versus Fig. 5C), increased MKP-1 activity could be responsible for the subsequent decrease in Ser10 phosphorylation either by dephosphorylating MAP kinases or histone H3-Ser10 itself (Kinney et al, 2009). Alternatively, the change in Ser10 phosphorylation may be regulating the transcription of MKP-1 (Li et al, 2001).…”

Section: Discussionmentioning

confidence: 93%

“…MKP-1 is a negative regulator of MAP kinase, hence a decrease in MAP kinase activity will result from induction of MKP-1 (Clark, 2003;Kuwano et al, 2008). In addition, MKP-1 can directly dephosphorylate P-H3-Ser10 in vitro (Kinney et al, 2009). However, in this model there was no induction of MKP-1 mRNA at the 5-g dose (Fig.…”

Section: Discussionmentioning

confidence: 99%

Histone H3 Phosphorylation (Ser10, Ser28) and Phosphoacetylation (K9S10) Are Differentially Associated with Gene Expression in Liver of Rats Treated In Vivo with Acute Ethanol

James¹,

Aroor²,

Lim³

et al. 2011

J Pharmacol Exp Ther

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The epigenetic histone modification by ethanol is emerging as one of the mechanisms for its deleterious effects in the liver. In this context, we have investigated the role of histone H3 phosphorylation at Ser10 (P-H3-Ser10), and Ser28 (P-H3-Ser28) in liver after acute ethanol treatment in vivo. Ethanol was administered intraperitoneally in male Sprague-Dawley rats. Ethanol dose-response (1-5 g/kg body weight) and time-course (1-4 h) experiments were conducted, and various parameters were monitored. Steatosis and necrosis (serum alanine aminotransferase) of the liver increased in 4 h, suggesting liver injury. There were differences between P-H3-Ser10 and P-H3-Ser28 at 1 h, with the latter being more sensitive to lower ethanol doses. It was noteworthy that phosphorylation of both serines disappeared at the highest dose used (5 g/kg). We also examined phosphoacetylation of histone H3 at K9S10 and observed a dramatic increase. The changes in histone H3 phosphorylation and phosphoacetylation were also accompanied with expression of early response genes (c-fos, c-jun, mitogen-activated protein kinase phosphatase-1). Chromatin immunoprecipitation assays in samples from 1.5 and 4 h of ethanol administration indicated that increased histone H3 phosphorylation at Ser28 was associated with the promoters of c-jun and plasminogen activator inhibitor-1. In conclusion, this study demonstrates for the first time that in vivo exposure of liver to acute ethanol induced phosphorylation and phosphoacetylation of histone H3, and these modifications are differentially involved in the mRNA expression of genes.

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“…For example, Aurora kinases A and B have been demonstrated to catalyze the addition of phosphate groups at H3S10, whereas mitogen-activated protein (MAP) kinase phosphatase-1 has previously been shown to promote the enzymatic removal of phosphate groups at this residue (Pascreau et al, 2003;Kinney et al, 2009). In brain, the dopamine and cAMP regulated protein phosphatase inhibitor, DARPP-32, as well as the MAP kinase, MSK1, provide excellent examples of enzymes regulating H3S10p in response to environmental stimuli, indicating histone phosphorylation as an important regulator of adult neuronal function (Brami-Cherrier et al, 2005;Stipanovich et al, 2008).…”

Section: Histone Phosphorylation and Cross Talk Interactions In The Cnsmentioning

confidence: 99%

Histone Regulation in the CNS: Basic Principles of Epigenetic Plasticity

Maze

Noh

Allis

2012

Neuropsychopharmacol

117

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Postmitotic neurons are subject to a vast array of environmental influences that require the nuclear integration of intracellular signaling events to promote a wide variety of neuroplastic states associated with synaptic function, circuit formation, and behavioral memory. Over the last decade, much attention has been paid to the roles of transcription and chromatin regulation in guiding fundamental aspects of neuronal function. A great deal of this work has centered on neurodevelopmental and adulthood plasticity, with increased focus in the areas of neuropharmacology and molecular psychiatry. Here, we attempt to provide a broad overview of chromatin regulation, as it relates to central nervous system (CNS) function, with specific emphasis on the modes of histone posttranslational modifications, chromatin remodeling, and histone variant exchange. Understanding the functions of chromatin in the context of the CNS will aid in the future development of pharmacological therapeutics aimed at alleviating devastating neurological disorders.

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Histone H3 as a novel substrate for MAP kinase phosphatase-1

Cited by 39 publications

References 60 publications

IκBα glutathionylation and reduced histone H3 phosphorylation inhibit eotaxin and RANTES

IκBα glutathionylation and reduced histone H3 phosphorylation inhibit eotaxin and RANTES

Histone H3 Phosphorylation (Ser10, Ser28) and Phosphoacetylation (K9S10) Are Differentially Associated with Gene Expression in Liver of Rats Treated In Vivo with Acute Ethanol

Histone Regulation in the CNS: Basic Principles of Epigenetic Plasticity

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