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    ItemOpen Access
    Data associated with "Lingual electrotactile discrimination ability is associated with the presence of specific connective tissue structures (papillae) on the tongue surface"
    (Colorado State University. Libraries, 2020) Allison, Tyler S.; Moritz, Joel, Jr.; Turk, Philip; Stone-Roy, Leslie M.
    Electrical stimulation of nerve endings in the tongue can be used to communicate information to users and has been shown to be highly effective in sensory substitution applications. The anterior tip of the tongue has very small somatosensory receptive fields, comparable to those of the fingertips, allowing for precise two-point discrimination and high tactile sensitivity. However, perception of electrotactile stimuli varies significantly between users, and across the tongue surface. Despite this, previous studies all used uniform electrode grids to stimulate a region of the dorsal-medial tongue surface. In an effort to customize electrode layouts for individual users, and thus improve efficacy for sensory substitution applications, we investigated whether specific neuroanatomical and physiological features of the tongue are associated with enhanced ability to perceive active electrodes. Specifically, the study described here was designed to test whether fungiform papillae density and/or propylthiouracil sensitivity are positively or negatively associated with perceived intensity and/or discrimination ability for lingual electrotactile stimuli. Fungiform papillae number and distribution were determined for 15 participants and they were exposed to patterns of electrotactile stimulation (ETS) and asked to report perceived intensity and perceived number of stimuli. Fungiform papillae number and distribution were then compared to ETS characteristics using comprehensive and rigorous statistical analyses. Our results indicate that fungiform papillae density is correlated with enhanced discrimination ability for electrical stimuli. In contrast, papillae density, on average, is not correlated with perceived intensity of active electrodes. However, results for at least one participant suggest that further research is warranted. Our data indicate that propylthiouracil taster status is not related to ETS perceived intensity or discrimination ability. These data indicate that individuals with higher fungiform papillae number and density in the anterior medial tongue region may be better able to use lingual ETS for sensory substitution.
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    ItemOpen Access
    Dataset associated with "The C2A domain of synaptotagmin is an essential component of the calcium sensor for synaptic transmission"
    (Colorado State University. Libraries, 2020) Bowers, Matthew; Reist, Noreen
    The synaptic vesicle protein, synaptotagmin, is the principle Ca2+ sensor for synaptic transmission. Ca2+ influx into active nerve terminals is translated into neurotransmitter release by Ca2+ binding to synaptotagmin's tandem C2 domains, triggering the fast, synchronous fusion of multiple synaptic vesicles. Two hydrophobic residues, shown to mediate Ca2+-dependent membrane insertion of these C2 domains, are required for this process. Previous research suggested that one of its tandem C2 domains (C2B) is critical for fusion, while the other domain (C2A) plays only a facilitatory role. However, the function of the two hydrophobic residues in C2A have not been adequately tested in vivo. Here we show that these two hydrophobic residues are absolutely required for synaptotagmin to trigger vesicle fusion. Using in vivo electrophysiological recording at the Drosophila larval neuromuscular junction, we found that mutation of these two key C2A hydrophoic residues almost completely abolished neurotransmitter release. Significantly, mutation of both hydrophobic residues resulted in more severe deficits than those seen in synaptotagmin null mutants. Thus, we report the most severe phenotype of a C2A mutation to date, demonstrating that the C2A domain is absolutely essential for synaptotagmin's function as the electrostatic switch.
  • No Thumbnail Available
    ItemOpen Access
    Dataset associated with "The role of the C2A domain of synaptotagmin 1 in asynchronous neurotransmitter release"
    (Colorado State University. Libraries, 2020) Shields, Mallory; Bowers, Matthew; Kramer, Hannah; Fulcer, McKenzie; Perinet, Lara; Metz, Marissa; Reist, Noreen
    Following 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.