Nucleosome-specific, Time-dependent Changes in Histone Modifications during Activation of the Early Growth Response 1 (Egr1) Gene

Riffo‐Campos, Ángela L.; Castillo, Josefa; Tur, Gema; González-Figueroa, Paula; Georgieva, Elena; Rodrı́guez, José Luis; López-Rodas, Gerardo; Rodrigo, M. Isabel; Franco, Luís

doi:10.1074/jbc.m114.579292

Cited by 20 publications

(29 citation statements)

References 59 publications

(66 reference statements)

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“…Although technical considerations precluded genomic analysis of H3S10ph induction at TSS, it clearly preceded H3 phosphoacetylation at remote regulatory sites. Analysis of specific genes confirmed the genomic data: H3S10 phosphorylation clearly preceded all the other TPA-induced histone modifications both at direct TCF-SRF target genes, consistent with a previous study of Egr1 (Riffo-Campos et al., 2015), and also at TCF-independent TPA-inducible genes. Taken together, our results support the notion that the hierarchy of changes in histone modifications observed in genomic analysis reflects the temporal order of their induction.…”

Section: Discussionsupporting

confidence: 91%

“…The MLL3/4 methyltransferase complexes control H3K4 methylation at enhancers (Hu et al., 2013), but MLL3 is detectable by ChIP at Egr1 , suggesting that it may act directly to influence H3K4me3 accumulation there. CHD2 is found at many TSS regions (Ernst and Kellis, 2013, Siggens et al., 2015) and may be required for signal-induced nucleosome remodeling events, which are known to accompany IE gene activation (Riffo-Campos et al., 2015). …”

Section: Discussionmentioning

confidence: 99%

“…In different contexts, H3 phosphorylation has been associated with recruitment of regulatory cofactors, chromatin modifiers, and remodelers (Cheung et al., 2000, Drobic et al., 2010, Josefowicz et al., 2016, Lo et al., 2000, Zippo et al., 2009), and with displacement of repressors (Lau and Cheung, 2011, Sawicka et al., 2014). For example, at mitogen-induced immediate-early genes, initial H3 phosphorylation is followed by nucleosome remodeling and appearance of H3K9ac and H3K4me3 as transcription increases (Drobic et al., 2010, Riffo-Campos et al., 2015, Zippo et al., 2007, Zippo et al., 2009). Nevertheless, the role played by specific transcription factors in the induction of chromatin modifications such as H3 phosphorylation, and their relationship to transcriptional activation, has remained unclear.…”

Section: Introductionmentioning

confidence: 99%

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ERK-Induced Activation of TCF Family of SRF Cofactors Initiates a Chromatin Modification Cascade Associated with Transcription

et al. 2017

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SummaryWe investigated the relationship among ERK signaling, histone modifications, and transcription factor activity, focusing on the ERK-regulated ternary complex factor family of SRF partner proteins. In MEFs, activation of ERK by TPA stimulation induced a common pattern of H3K9acS10ph, H4K16ac, H3K27ac, H3K9acK14ac, and H3K4me3 at hundreds of transcription start site (TSS) regions and remote regulatory sites. The magnitude of the increase in histone modification correlated well with changes in transcription. H3K9acS10ph preceded the other modifications. Most induced changes were TCF dependent, but TCF-independent TSSs exhibited the same hierarchy, indicating that it reflects gene activation per se. Studies with TCF Elk-1 mutants showed that TCF-dependent ERK-induced histone modifications required Elk-1 to be phosphorylated and competent to activate transcription. Analysis of direct TCF-SRF target genes and chromatin modifiers confirmed this and showed that H3S10ph required only Elk-1 phosphorylation. Induction of histone modifications following ERK stimulation is thus directed by transcription factor activation and transcription.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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ERK-Induced Activation of TCF Family of SRF Cofactors Initiates a Chromatin Modification Cascade Associated with Transcription

et al. 2017

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“…Therefore, it appears that lasting cellular changes in synaptic plasticity can be triggered by a transient histone modification signal. Rapid, stimulation-induced changes in histone modifications at promoters of genes have been previously described in other model systems [6, 25, 32]. …”

Section: Discussionmentioning

confidence: 89%

Proteasome regulates transcription-favoring histone methylation, acetylation and ubiquitination in long-term synaptic plasticity

Tacon

Morgan

Hegde

2015

Neuroscience Letters

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Histone modifications, such as lysine methylation, acetylation and ubiquitination, are epigenetic tags that shape the chromatin landscape and regulate transcription required for synaptic plasticity and memory. Here we show that transcription-promoting histone H3 trimethylated at lysine 4 (H3K4me3), histone H3 acetylated at lysine 9 and 14 (H3K9/14ac), and histone H2B monoubiquitinated at lysine 120 (H2BK120ub) are enhanced after the induction of long-lasting chemically-induced long-term potentiation (cLTP) in the murine hippocampus. While H3K4me3 and H3K9/14ac were transiently upregulated, H2BK120ub levels oscillated after cLTP induction. In addition, we present results showing that blocking the proteasome, a molecular complex specialized for targeted protein degradation, inhibited the upregulation of these epigenetic tags after cLTP. Thus, our study provides the initial steps towards understanding the role of the proteasome in regulating histone modifications critical for synaptic plasticity.

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“…The experiments reported earlier described histone modifications that lasted hours or days after synaptic stimulation or behavioral training (Gupta-Agarwal et al, 2012; Levenson et al, 2004). It has also been shown, however, that histone modifications can occur rapidly, in minutes (Buro et al, 2010; Lopez-Atalaya et al, 2013; Riffo-Campos et al, 2015). Some researchers have postulated that lasting cellular changes in synaptic plasticity can be triggered by a transient histone modification signal (Levenson and Sweatt, 2005).…”

Section: The Upp and Long-term Synaptic Plasticitymentioning

confidence: 99%

Proteolysis, synaptic plasticity and memory

Hegde

2017

Neurobiology of Learning and Memory

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Protein degradation has many critical functions in the nervous system such as refinement of synaptic connections during development and synaptic plasticity and memory in the adult organisms. A major cellular machinery of proteolysis is the ubiquitin-proteasome pathway (UPP). The UPP precisely regulates proteolysis by covalently attaching ubiquitin, a small protein, to substrates through sequential enzymatic reactions and the proteins marked with the ubiquitin tag are degraded by complex containing many subunits called the proteasome. Research over the years has shown a role for the UPP in regulating presynaptic and postsynaptic proteins critical for neurotransmission and synaptic plasticity. Studies have also revealed a role for the UPP in various forms of memory. Mechanistic investigations suggest that the function of the UPP in neurons is not homogenous and is subject to local regulation in different neuronal sub-compartments. In both invertebrate and vertebrate model systems, local roles have been found for enzymes that attach ubiquitin to substrate proteins as well as for enzymes that remove ubiquitin from substrates. The proteasome also has disparate functions in different parts of the neuron. In addition to the UPP, proteolysis by the lysosome and autophagy play a role in synaptic plasticity and memory. This review details the functions of proteolysis in synaptic plasticity and summarizes the findings on the connection between proteolysis and memory mainly focusing on the UPP including its local roles.

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Nucleosome-specific, Time-dependent Changes in Histone Modifications during Activation of the Early Growth Response 1 (Egr1) Gene

Cited by 20 publications

References 59 publications

ERK-Induced Activation of TCF Family of SRF Cofactors Initiates a Chromatin Modification Cascade Associated with Transcription

ERK-Induced Activation of TCF Family of SRF Cofactors Initiates a Chromatin Modification Cascade Associated with Transcription

Proteasome regulates transcription-favoring histone methylation, acetylation and ubiquitination in long-term synaptic plasticity

Proteolysis, synaptic plasticity and memory

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