Abstract
Elongator protein 3 (ELP3) acetylates histones in the nucleus but also plays a role in the cytoplasm. Here, we report that in Drosophila neurons, ELP3 is necessary and sufficient to acetylate the ELKS family member Bruchpilot, an integral component of the presynaptic density where neurotransmitters are released. We find that in elp3 mutants, presynaptic densities assemble normally, but they show morphological defects such that their cytoplasmic extensions cover a larger area, resulting in increased vesicle tethering as well as a more proficient neurotransmitter release. We propose a model where ELP3-dependent acetylation of Bruchpilot at synapses regulates the structure of individual presynaptic densities and neurotransmitter release efficiency.
Copyright © 2011 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Acetyltransferases*
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Animals
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Animals, Genetically Modified
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Cell Line, Transformed
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Drosophila
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Drosophila Proteins / genetics
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Drosophila Proteins / metabolism*
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Embryo, Mammalian
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Green Fluorescent Proteins / genetics
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Histone Acetyltransferases / genetics
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Histone Acetyltransferases / metabolism*
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Humans
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Larva
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Microscopy, Electron, Transmission
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Mutation / genetics
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Neuromuscular Junction / metabolism*
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Neuromuscular Junction / physiology
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Patch-Clamp Techniques
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Presynaptic Terminals / physiology*
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Presynaptic Terminals / ultrastructure
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Transfection / methods
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Tubulin / metabolism
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Zebrafish
Substances
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BRP protein, Drosophila
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Drosophila Proteins
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Nerve Tissue Proteins
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Tubulin
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Green Fluorescent Proteins
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Acetyltransferases
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ELP3 protein, Drosophila
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Histone Acetyltransferases