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https://doi.org/10.1523/ENEURO.0019-14.2014
Title: | Nuclear arc interacts with the histone acetyltransferase Tip60 to modify H4K12 acetylation | Authors: | Wee, C.L Teo, S Oey, N.E Wright, G.D VanDongen, H.M.A VanDongen, A.M.J |
Issue Date: | 2014 | Citation: | Wee, C.L, Teo, S, Oey, N.E, Wright, G.D, VanDongen, H.M.A, VanDongen, A.M.J (2014). Nuclear arc interacts with the histone acetyltransferase Tip60 to modify H4K12 acetylation. eNeuro 1 (1) : e0019-14.2014. ScholarBank@NUS Repository. https://doi.org/10.1523/ENEURO.0019-14.2014 | 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. © 2014 Wee et al. | Source Title: | eNeuro | URI: | https://scholarbank.nus.edu.sg/handle/10635/176168 | ISSN: | 2373-2822 | DOI: | 10.1523/ENEURO.0019-14.2014 |
Appears in Collections: | Elements Staff Publications |
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