Abstract
Munc13 proteins are essential in neurotransmitter release, controlling the priming of synaptic vesicles to a release-ready state. The sequences responsible for this priming activity are unknown. Here we identify a large alpha-helical domain of mammalian Munc13-1 that is autonomously folded and is sufficient to rescue the total arrest in neurotransmitter release observed in hippocampal neurons lacking Munc13s.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chromatography, Gel
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Computational Biology
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Excitatory Postsynaptic Potentials
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Exocytosis / genetics
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Exocytosis / physiology*
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Gene Expression*
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Hippocampus / metabolism*
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Mice
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Mice, Knockout
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Nerve Tissue Proteins / genetics*
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Nerve Tissue Proteins / metabolism
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Neurons / drug effects
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Neurons / metabolism*
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Neurotransmitter Agents / metabolism
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Nuclear Magnetic Resonance, Biomolecular
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Protein Folding
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Protein Structure, Secondary / genetics
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Protein Structure, Tertiary
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Rats
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Structure-Activity Relationship
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Sucrose / pharmacology
Substances
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Nerve Tissue Proteins
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Neurotransmitter Agents
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Unc13a protein, rat
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Sucrose