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Dataset associated with "The role of the C2A domain of synaptotagmin 1 in asynchronous neurotransmitter release"

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dc.contributor.authorShields, Mallory
dc.contributor.authorBowers, Matthew
dc.contributor.authorKramer, Hannah
dc.contributor.authorFulcer, McKenzie
dc.contributor.authorPerinet, Lara
dc.contributor.authorMetz, Marissa
dc.contributor.authorReist, Noreen
dc.coverage.spatialFort Collins (Colo.)en_US
dc.coverage.temporal2015-2018en_US
dc.date.accessioned2020-04-17T16:48:12Z
dc.date.available2020-04-17T16:48:12Z
dc.date.issued2020
dc.descriptionThis dataset includes all raw data for experiments included in the manuscript. It also includes raw, unedited microscopy and blot images.en_US
dc.descriptionCollege of Veterinary Medicine and Biomedical Sciences
dc.descriptionDepartment of Biomedical Sciences
dc.description.abstractFollowing nerve stimulation, there are two distinct phases of Ca2+-dependent neurotransmitter release: a fast, synchronous release phase, and a prolonged, asynchronous release phase. Each of these phases is tightly regulated and mediated by distinct mechanisms. Synaptotagmin 1 is the major Ca2+ sensor that triggers fast, synchronous neurotransmitter release upon Ca2+ binding by its C2A and C2B domains. It has also been implicated in the inhibition of asynchronous neurotransmitter release, as blocking Ca2+ binding by the C2A domain of synaptotagmin 1 results in increased asynchronous release. However, the mutation used to block Ca2+ binding in the previous experiments (aspartate to asparagine mutations, sytD-N) had the unintended side effect of mimicking Ca2+ binding, raising the possibility that the increase in asynchronous release was directly caused by ostensibly constitutive Ca2+ binding. Thus, rather than modulating an asynchronous sensor, sytD-N may be mimicking one. To directly test this C2A inhibition hypothesis, we utilized an alternate C2A mutation that we designed to block Ca2+ binding without mimicking it (an aspartate to glutamate mutation, sytD-E). Analysis of both the original sytD-N mutation and our alternate sytD-E mutation at the Drosophila neuromuscular junction showed differential effects on asynchronous release, as well as on synchronous release and the frequency of spontaneous release. Importantly, we found that asynchronous release is not increased in the sytD-E mutant. Thus, our work provides new mechanistic insight into synaptotagmin 1 function during Ca2+-evoked synaptic transmission and demonstrates that Ca2+ binding by the C2A domain of synaptotagmin 1 does not inhibit asynchronous neurotransmitter release in vivo.en_US
dc.description.sponsorshipNER is funded by the National Science Foundation (1257363) and a Colorado State University (CSU) College of Veterinary Medicine and Biomedical Sciences College Research Council award. MCS is funded through the Vice President for Research Fellowship at CSU.en_US
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dc.identifier.urihttps://hdl.handle.net/10217/204914
dc.identifier.urihttp://dx.doi.org/10.25675/10217/204914
dc.languageEnglishen_US
dc.language.isoengen_US
dc.publisherColorado State University. Librariesen_US
dc.relation.ispartofResearch Data
dc.relation.isreferencedbyShields MC, Bowers MR, Kramer HL, Fulcer MM, Perinet LC, Metz MJ, et al. (2020) The role of the C2A domain of synaptotagmin 1 in asynchronous neurotransmitter release. PLoS ONE 15(5): e0232991. https://doi.org/10.1371/journal.pone.0232991en_US
dc.subjectsynapse
dc.subjectneuroscience
dc.subjectvesicle fusion
dc.subjectneurotransmitter release
dc.subjectsynaptotagmin
dc.subjectasynchronous release
dc.titleDataset associated with "The role of the C2A domain of synaptotagmin 1 in asynchronous neurotransmitter release"en_US
dc.typeDataseten_US

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