Depolarization induces acetylation of histone H2B in the hippocampus

Maharana, Chinmoyee; Sharma, Kaushik; Sharma, Shiv K.

doi:10.1016/j.neuroscience.2010.02.023

Cited by 25 publications

(22 citation statements)

References 54 publications

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“…Interestingly, a downregulation of only H2B histone acetylation was found in the hippocampus of cbp + /À mice (Alarcon et al, 2004), and H2B was also identified as a substrate for p300 and PCAF, but not Tip60 (Roth et al, 2001;Allis et al, 2007). At the mechanistic level, a recent paper described the acetylation of H2B in response to depolarization in hippocampal slices in vitro (Maharana et al, 2010). This is in line with our study enlightening the implication of glutamatergicFat least in part with cholinergicFprojections in the control of H2B acetylation and further strengthened its potential role in memory formation.…”

Section: Discussionmentioning

confidence: 99%

Spatial Memory Consolidation is Associated with Induction of Several Lysine-Acetyltransferase (Histone Acetyltransferase) Expression Levels and H2B/H4 Acetylation-Dependent Transcriptional Events in the Rat Hippocampus

Bousiges

Vasconcelos

Neidl

et al. 2010

Neuropsychopharmacol

161

142

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Numerous genetic studies have shown that the CREB-binding protein (CBP) is an essential component of long-term memory formation, through its histone acetyltransferase (HAT) function. E1A-binding protein p300 and p300/CBP-associated factor (PCAF) have also recently been involved in memory formation. By contrast, only a few studies have reported on acetylation modifications during memory formation, and it remains unclear as to how the system is regulated during this dynamic phase. We investigated acetylation-dependent events and the expression profiles of these HATs during a hippocampus-dependent task taxing spatial reference memory in the Morris water maze. We found a specific increase in H2B and H4 acetylation in the rat dorsal hippocampus, while spatial memory was being consolidated. This increase correlated with the degree of specific acetylated histones enrichment on some memory/plasticity-related gene promoters. Overall, a global increase in HAT activity was measured during this memory consolidation phase, together with a global increase of CBP, p300, and PCAF expression. Interestingly, these regulations were altered in a model of hippocampal denervation disrupting spatial memory consolidation, making it impossible for the hippocampus to recruit the CBP pathway (CBP regulation and acetylated-H2B-dependent transcription). CBP has long been thought to be present in limited concentrations in the cells. These results show, for the first time, that CBP, p300, and PCAF are dynamically modulated during the establishment of a spatial memory and are likely to contribute to the induction of a specific epigenetic tagging of the genome for hippocampus-dependent (spatial) memory consolidation. These findings suggest the use of HAT-activating molecules in new therapeutic strategies of pathological aging, Alzheimer's disease, and other neurodegenerative disorders.

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Section: Discussionmentioning

confidence: 99%

Spatial Memory Consolidation is Associated with Induction of Several Lysine-Acetyltransferase (Histone Acetyltransferase) Expression Levels and H2B/H4 Acetylation-Dependent Transcriptional Events in the Rat Hippocampus

Bousiges

Vasconcelos

Neidl

et al. 2010

Neuropsychopharmacol

161

142

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“…Histone acetylation is triggered by several forms of neuronal activity. Potassium chloride-mediated neuronal depolarization, and stimulation by dopaminergic, cholinergic and glutamatergic pathways all increase the acetylation of H2B, H3K14 and H3S10 [279,280].In these cases, all changes in histone acetylation occurred in parallel to phosphorylation events and direct activation of the MAPK-ERK-pathway [281,282], indicating a crosstalk between H3K14 acetylation and H3S10 phosphorylation events [272,282]. Neuronal activity also starts a positive-feedback loop of HDAC2 and brainderived neurotropic factor (BDNF).…”

Section: Lysine Acetylation and Cognitive Declinementioning

confidence: 99%

The world of protein acetylation

Drazic

Myklebust

Ree

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

646

532

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Acetylation is one of the major post-translational protein modifications in the cell, with manifold effects on the protein level as well as on the metabolome level. The acetyl group, donated by the metabolite acetyl-coenzyme A, can be co- or post-translationally attached to either the α-amino group of the N-terminus of proteins or to the ε-amino group of lysine residues. These reactions are catalyzed by various N-terminal and lysine acetyltransferases. In case of lysine acetylation, the reaction is enzymatically reversible via tightly regulated and metabolism-dependent mechanisms. The interplay between acetylation and deacetylation is crucial for many important cellular processes. In recent years, our understanding of protein acetylation has increased significantly by global proteomics analyses and in depth functional studies. This review gives a general overview of protein acetylation and the respective acetyltransferases, and focuses on the regulation of metabolic processes and physiological consequences that come along with protein acetylation.

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“…Hippocampal slice preparation and recovery were carried out as described earlier (Maharana et al 2010). Slices from both the hippocampi of an animal were pooled and randomly distributed into treatment groups, with 3-4 slices in each group.…”

Section: Methodsmentioning

confidence: 99%

“…Slices from both the hippocampi of an animal were pooled and randomly distributed into treatment groups, with 3-4 slices in each group. KCl treatment of hippocampal slices was performed with 90 mM KCl (Wu et al 2001;Maharana et al 2010) in artificial cerebrospinal fluid (aCSF) for 10 min. The concentration of NaCl in KCl-aCSF was correspondingly reduced.…”

Section: Methodsmentioning

confidence: 99%

“…The NMDA receptor blocker, 2-amino-5-phosphonovaleric acid (APV; Calbiochem) was used at 50 μM concentration (Roberson and Sweatt 1996) 30 min before and during NMDA treatment. After the treatments, area CA1 was isolated and processed for Western blotting and signal detection as described earlier (Maharana et al 2010). Insular cortex region was isolated based on the rat brain atlas of Paxinos and Watson (1986) and treated with 1.65 μM TSA (Calbiochem; Levenson et al 2004) for 2 h. The level of acetylated p55 protein was assessed using the acetyl-lysine antibody (Cell Signaling Technology).…”

Section: Methodsmentioning

confidence: 99%

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Activity-Dependent Acetylation of Alpha Tubulin in the Hippocampus

Pandey

Sharma

2011

J Mol Neurosci

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Posttranslational modifications in proteins play critical roles in synaptic plasticity and memory. In addition, the enduring form of long-term potentiation (LTP) and long-term memory require synthesis of proteins. Some of the mRNAs are present in the dendrites and are locally translated into proteins. Microtubules play critical roles in neuronal transport including the transport of mRNAs from the cell body to the dendrites. Here, we show that KCl depolarization increases acetylation of α-tubulin, a constituent of microtubules, in the CA1 region of the hippocampal slices. Furthermore, activation of N-methyl-D: -aspartate receptor, a type of glutamate receptor that plays critical roles in LTP and memory, also enhances α-tubulin acetylation. These results show that acetylation of α-tubulin is modulated in an activity-dependent manner.

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Depolarization induces acetylation of histone H2B in the hippocampus

Cited by 25 publications

References 54 publications

Spatial Memory Consolidation is Associated with Induction of Several Lysine-Acetyltransferase (Histone Acetyltransferase) Expression Levels and H2B/H4 Acetylation-Dependent Transcriptional Events in the Rat Hippocampus

Spatial Memory Consolidation is Associated with Induction of Several Lysine-Acetyltransferase (Histone Acetyltransferase) Expression Levels and H2B/H4 Acetylation-Dependent Transcriptional Events in the Rat Hippocampus

The world of protein acetylation

Activity-Dependent Acetylation of Alpha Tubulin in the Hippocampus

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