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Research ArticleNew Research, Neuronal Excitability

Nuclear Arc Interacts with the Histone Acetyltransferase Tip60 to Modify H4K12 Acetylation

Caroline L. Wee, Shaun Teo, Nicodemus E. Oey, Graham D. Wright, Hendrika M.A. VanDongen and Antonius M.J. VanDongen
eNeuro 12 November 2014, 1 (1) ENEURO.0019-14.2014; https://doi.org/10.1523/ENEURO.0019-14.2014
Caroline L. Wee
1Program in Neuroscience and Behavioral Disorders, Duke-NUS Graduate Medical School, Singapore 169857
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Shaun Teo
1Program in Neuroscience and Behavioral Disorders, Duke-NUS Graduate Medical School, Singapore 169857
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Nicodemus E. Oey
1Program in Neuroscience and Behavioral Disorders, Duke-NUS Graduate Medical School, Singapore 169857
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Graham D. Wright
2Institute of Medical Biology, a*STAR, Singapore 138648
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Hendrika M.A. VanDongen
1Program in Neuroscience and Behavioral Disorders, Duke-NUS Graduate Medical School, Singapore 169857
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Antonius M.J. VanDongen
1Program in Neuroscience and Behavioral Disorders, Duke-NUS Graduate Medical School, Singapore 169857
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Abstract

Arc is an immediate-early gene whose genetic ablation selectively abrogates long-term memory, indicating a critical role in memory consolidation. Although Arc protein is found at synapses, it also localizes to the neuronal nucleus, where its function is less understood. Nuclear Arc forms a complex with the β-spectrin isoform βSpIVΣ5 and associates with PML bodies, sites of epigenetic regulation of gene expression. We report here a novel interaction between Arc and Tip60, a histone-acetyltransferase and subunit of a chromatin-remodelling complex, using biochemistry and super-resolution microscopy in primary rat hippocampal neurons. Arc and βSpIVΣ5 are recruited to nuclear Tip60 speckles, and the three proteins form a tight complex that localizes to nuclear perichromatin regions, sites of transcriptional activity. Neuronal activity-induced expression of Arc (1) increases endogenous nuclear Tip60 puncta, (2) recruits Tip60 to PML bodies, and (3) increases histone acetylation of Tip60 substrate H4K12, a learning-induced chromatin modification. These mechanisms point to an epigenetic role for Arc in regulating memory consolidation.

  • chromatin modification
  • epigenetics
  • histone acetylation
  • immediate early gene
  • synaptic plasticity

Footnotes

  • ↵1 The authors report no financial conflicts of interest.

  • ↵3 This work was supported by Grant MOE2012-T2-1-039 from the Singapore Ministry of Education to A.M.J.V.D. and an award from the Singapore Ministry of Health and A*STAR, the Agency for Science, Technology and Research. The SIM experiments were performed at the IMB Microscopy Unit, Institute of Medical Biology, A*STAR. The STED and STORM experiments were performed at the SingHealth Advanced Bio-imaging Core facility.

This is an open-access article distributed under the terms of the Creative Commons Attribution License Attribution-Noncommercial 4.0 International which permits noncommercial reuse provided that the original work is properly attributed.

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Nuclear Arc Interacts with the Histone Acetyltransferase Tip60 to Modify H4K12 Acetylation
Caroline L. Wee, Shaun Teo, Nicodemus E. Oey, Graham D. Wright, Hendrika M.A. VanDongen, Antonius M.J. VanDongen
eNeuro 12 November 2014, 1 (1) ENEURO.0019-14.2014; DOI: 10.1523/ENEURO.0019-14.2014

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Nuclear Arc Interacts with the Histone Acetyltransferase Tip60 to Modify H4K12 Acetylation
Caroline L. Wee, Shaun Teo, Nicodemus E. Oey, Graham D. Wright, Hendrika M.A. VanDongen, Antonius M.J. VanDongen
eNeuro 12 November 2014, 1 (1) ENEURO.0019-14.2014; DOI: 10.1523/ENEURO.0019-14.2014
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Keywords

  • Chromatin Modification
  • epigenetics
  • Histone Acetylation
  • immediate early gene
  • synaptic plasticity

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