Glutamate induces histone H3 phosphorylation but not acetylation in striatal neurons: role of mitogen‐ and stress‐activated kinase‐1

Brami‐Cherrier, Karen; Lavaur, Jérémie; Pagès, Christiane; Arthur, J. Simon C.; Caboche, Jocelyne

doi:10.1111/j.1471-4159.2006.04352.x

Cited by 64 publications

(68 citation statements)

References 34 publications

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“…Earlier analyses on histone acetylation in response to cocaine (Brami-Cherrier et al, 2007, 2005Cassel et al, 2006) or ethanol (Kim and Shukla, 2006;Pandey et al, 2008) have produced somewhat conflicting results. Despite the dose-dependent hyperacetylation observed in response to sodium butyrate, our analysis failed to reveal significant changes in bulk chromatin acetylation after acute administration of cocaine, ethanol, or morphine to saline or sodium butyrate-pretreated mice.…”

Section: Discussionmentioning

confidence: 98%

Selective Boosting of Transcriptional and Behavioral Responses to Drugs of Abuse by Histone Deacetylase Inhibition

Sanchis‐Segura

López‐Atalaya

Barco

2009

Neuropsychopharmacol

121

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Histone acetylation and other modifications of the chromatin are important regulators of gene expression and, consequently, may contribute to drug-induced behaviors and neuroplasticity. Earlier studies have shown that a reduction in histone deacetylase (HDAC) activity results in the enhancement of some psychostimulant-induced behaviors. In this study, we extend those seminal findings by showing that the administration of the HDAC inhibitor sodium butyrate enhances morphine-induced locomotor sensitization and conditioned place preference. In contrast, this compound has no effects on the development of morphine tolerance and dependence. Similar effects were observed for cocaine and ethanol-induced behaviors. These behavioral changes were accompanied by a selective boosting of a component of the transcriptional program activated by chronic morphine administration that included circadian clock genes and other genes relevant to addictive behavior. Our results support a specific function for histone acetylation and the epigenetic modulation of transcription at a reduced number of biologically relevant loci on non-homeostatic, long-lasting, drug-induced behavioral plasticity.

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Section: Discussionmentioning

confidence: 98%

Selective Boosting of Transcriptional and Behavioral Responses to Drugs of Abuse by Histone Deacetylase Inhibition

Sanchis‐Segura

López‐Atalaya

Barco

2009

Neuropsychopharmacol

121

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“…We observed that some important nuclear events driven by activated ERKs were not affected by the peptide, namely phosphorylation of MSK-1, CREB and histone H3. MSK-1 is a direct nuclear target of ERK with no DEF domain (Sharrocks et al, 2000), critically involved in both CREB and histone H3 phosphorylation in striatal neurons (Brami-Cherrier et al, 2005, 2007. As a consequence, the pattern of gene expression induced by glutamate was differently affected by the TAT-DEF-Elk-1 peptide compared with a classical MEK inhibitor, which had a more widespread effect.…”

Section: Discussionmentioning

confidence: 99%

“…For this purpose, we chose IEGs that are controlled by the ERK cascade via their SRE and/or CRE binding domains (namely c-Fos, Zif268 and JunB) or via histone H3 phosphorylation (namely c-Jun) (supplemental Fig. 1, available at www.jneurosci.org as supplemental material) (Brami-Cherrier et al, 2007). The U0126 compound had a profound inhibitory role on glutamate-induced c-Fos, Zif268 and JunB induced expression (Fig.…”

Section: Comparative Effects Of Mek Inhibitor and Tat-def-elk-1 Peptimentioning

confidence: 99%

A TAT–DEF–Elk-1 Peptide Regulates the Cytonuclear Trafficking of Elk-1 and Controls Cytoskeleton Dynamics

Lavaur¹,

Bernard²,

Trifilieff³

et al. 2007

J. Neurosci.

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The transcription factor Elk-1 plays a key role in cell differentiation, proliferation and apoptosis. This role is thought to arise from its phosphorylation by activated extracellular signal-regulated kinases (ERKs), a critical posttranslational event for the transcriptional activity of the ternary complex composed of Elk-1 and a dimer of serum response factor (SRF) at the serum response element (SRE) regulatory site of transcription. In addition to its nuclear localization, Elk-1 is found in the dendrites and soma of neuronal cells and recent evidence implicate a cytoplasmic proapoptotic function of Elk-1, via its association with the mitochondrial permeability transition pore complex. Thus, the nuclear versus cytoplasmic localization of Elk-1 seems to be crucial for its biological function. In this study we show that the excitatory neurotransmitter, glutamate, induces an ERK-dependent Elk-1 activation and nuclear relocalization. We demonstrate that Elk-1 phosphorylation on Ser383/389 has a dual function and triggers both Elk-1 nuclear translocation and SRE-dependent gene expression. Mutating these sites into inactive residues or using a synthetic penetrating peptide (TAT-DEF-Elk-1), which specifically interferes with the DEF docking domain of Elk-1, prevents Elk-1 nuclear translocation without interfering with ERK nor MSK1 (mitogenand stress-activated protein kinase 1), a CREB kinase downstream from ERK-activation. This results in a differential regulation of glutamate-induced IEG regulation when compared with classical inhibitors of the ERK pathway. Using the TAT-DEF-Elk-1 peptide or the dominant-negative version of Elk-1, we show that Elk-1 phosphorylation controls dendritic elongation, SRF and Actin expression levels as well as cytoskeleton dynamics.

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“…It is well known that mitogen-and stress-activated kinase 1 (MSK1), a kinase downstream of ERK, plays an important role in modification of histone H3 [23,24]. We examined whether MSK1 is phosphorylated during treatment with quercetin.…”

Section: Erk Mediates the Phosphorylation Of Msk1 By Quercetinmentioning

confidence: 99%

Quercetin augments TRAIL-induced apoptotic death: Involvement of the ERK signal transduction pathway

Kim

Lee

Jeong

et al. 2008

Biochemical Pharmacology

157

115

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Combined treatment with quercetin and TRAIL induced cytotoxicity and enhanced annexin V staining and poly (ADP-ribose) polymerase (PARP) cleavage in human prostate cancer cell lines DU-145 and PC-3. These indicators of apoptosis resulted from the activation of caspase-8, -9, and -3. Although the expression levels of FLIPs, cIAP1, cIAP2, and the Bcl-2 family were not changed in quercetin-treated cells, significant downregulation of survivin occurred. Knockdown survivin by siRNA significantly increased TRAIL-induced apoptosis. We hypothesized that quercetin-induced activation of MAPK (ERK, p38, JNK) is responsible for downregulation of survivin gene expression. To test this hypothesis, we selectively inhibited MAPK during treatment with quercetin. Our data demonstrated that inhibitor of ERK (PD98059), but not p38 MAPK (SB203580) or JNK (SP600125), significantly maintained the intracellular level of survivin during treatment with quercetin. Interestingly, PD98059 also prevented quercetin-induced deacetylation of histone H3. Data from survivin promoter activity assay suggest that the Sp1 transcription factor binds to the survivin promoter region and quercetin inhibits its binding activity through deacetylation of histone H3. Quercetin-induced activation of the ERK-MSK1 signal transduction pathway may be responsible for deacetylation of histone H3. Taken together, our findings suggest that quercetin enhances TRAIL induced apoptosis by inhibition of survivin expression, through ERK-MSK1-mediated deacetylation of H3.

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Glutamate induces histone H3 phosphorylation but not acetylation in striatal neurons: role of mitogen‐ and stress‐activated kinase‐1

Cited by 64 publications

References 34 publications

Selective Boosting of Transcriptional and Behavioral Responses to Drugs of Abuse by Histone Deacetylase Inhibition

Selective Boosting of Transcriptional and Behavioral Responses to Drugs of Abuse by Histone Deacetylase Inhibition

A TAT–DEF–Elk-1 Peptide Regulates the Cytonuclear Trafficking of Elk-1 and Controls Cytoskeleton Dynamics

Quercetin augments TRAIL-induced apoptotic death: Involvement of the ERK signal transduction pathway

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