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Munc13-1 and Munc18-1, but not CAPS-1/2, stabilize primed synaptic vesicles by preventing NSF-dependent de-priming.
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Data suggest that the Munc13-1/2 heterodimer is an active component of the vesicle docking, priming and release complex.
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In a model of systemic anaphylaxis, we found no difference between WT and Munc13-2 KO mice, but global and mast cells-specific Munc13-4 KO mice developed less hypothermia. We conclude that although Munc13-2 plays a minor role, Munc13-4 is essential for regulated exocytosis in mast cells
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Mutating Ca(2+)-coordinating aspartates in the C2A-domain localizes Doc2B permanently at the plasma membrane, and renders an upstream priming step Ca(2+)-independent, whereas a separate function in downstream priming depends on SNARE-binding, Ca(2+)-binding to the C2B-domain of Doc2B, interaction with ubMunc13-2 and the presence of synaptotagmin-1.
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This study characterizes Munc13-1 as a target of resveratrol and highlights the importance of dietary polyphenol in the management of neurodegenerative diseases
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SIGNIFICANCE STATEMENT: DBA/2J and C57BL/6J mice have been used to understand the genetic mechanisms controlling behaviors related to a number of psychiatric illnesses. However, the fundamental neurobiological mechanisms producing these behavioral characteristics remain unresolved. Here we identify a critical family of presynaptic proteins differentially expressed by these strains that control strain-dependent synaptic ph
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Munc13-2 is recruited to synapses by the AZ protein ELKS1.
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Munc13-2 plays a fundamental role in large dense-core vesicle exocytosis, but in contrast to synapses lacking Munc13s, the corresponding chromaffin cells do not exhibit a vesicle docking defect.
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Data demonstrate that Munc13-1 and DOC2B have different effects on network activity and that by enhancing asynchronous release, DOC2B exerts its properties to increase spiking activity and elevate synchronization between neurons within network bursts
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Munc13-1 isoform is functionaly redundant in cytotoxic T lymphocytes.
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betaARs couple to a cAMP/Epac/PLC/Munc13-1/Rab3a/RIM1a-dependent pathway to enhance glutamate release at cerebrocortical nerve terminals.
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Our data establish Munc13-1 as a major presynaptic target of Ca(2+)-Calmodulin signaling and show that the Ca(2+)-Calmodulin-Munc13-1 complex is a pivotal component of the molecular machinery that determines short-term synaptic plasticity characteristics.
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The Munc13 gene family encodes molecules located at the synaptic active zone that regulate the reliability of synapses to encode information over a wide range of frequencies in response to action potentials.
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This study demonistrated that Munc13 genotype regulates secretory amyloid precursor protein processing via postsynaptic glutamate receptors
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Mammalian homologue of Caenorhabditis elegans unc-13-1 (Munc13-1) plays a role in the recruitment of newcomer insulin granules in both first and second phases of glucose-stimulated insulin secretion in mouse islets.
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Munc13-1/2 were shown to facilitate dense-core vesicle fusion but, unlike for synaptic vesicles, were not essential for dense-core vesicle release.
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The composition of Munc13 isoforms in a neuron differentially controls its short-term synaptic plasticity characteristics.
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photoreceptor ribbon synapses and conventional synapses differ fundamentally with regard to their dependence on synaptic vesicles priming proteins of the Munc13 family
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Disruption of Munc13-1 function inhibits mossy fiber long-term potentiation
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Data show that homodimerization of Munc13 inhibits its synaptic vesicle priming function, and RIMs activate priming by disrupting Munc13 homodimerization.
