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7 results for “Synaptotagmin-1”
Dataset for the Synaptotagmin-1 antibody screening study
<p><strong>This antibody characterization dataset is related to the F1000 research article openly available at F1000Research.</strong></p> <p><em>The dataset presented contains the following underlying raw data for study which evaluated twelve commercial antibodies against Synaptotagmin-1 in western blot, immunoprecipitation, immunofluorescence and flow cytometry. The original study is also accessible on the YCharOS Zenodo community (<a href="https://doi.org/10.5281/zenodo.12666747">https://doi.org/10.5281/zenodo.12666747</a>).</em></p> <p><em>The Dataset is in the format of a zip file. Once downloaded, please expand the zip file to access the folders containing the underlying data for Western blot (Wb), immunoprecipitation (IP) and immunofluorescence (IF).</em></p>
Molecular dynamics dataset of Synaptotagmin-1
<p>This dataset contains all-atom molecular dynamics trajectories of synaptotagmin-1 C2A (calcium free). Each trajectory is 2 µs long and the total cumulated simulation time is 184 µs. Details, including the molecular dynamics setup, are given in Hempel, T.; Plattner, N.; Noé, F. Coupling of Conformational Switches in Calcium Sensor Unraveled with Local Markov Models and Transfer Entropy. <em>J. Chem. Theory Comput.</em> <strong>2020</strong>, <em>16</em> (4), 2584–2593. <a href="https://doi.org/10.1021/acs.jctc.0c00043">https://doi.org/10.1021/acs.jctc.0c00043</a>.</p>
A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release and Studies of Synaptotagmin-1 action by all-atom molecular dynamics simulations
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NMR data in 'Ca2+-dependent release of Synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes' by Voleti, Jaczynska and Rizo, eLife 2020
<p>The Ca<sup>2+</sup> sensor synaptotagmin-1 and the SNARE complex cooperate to trigger neurotransmitter release. Structural studies elucidated three distinct synaptotagmin-1-SNARE complex binding modes involving 'polybasic', 'primary' and 'tripartite' interfaces of synaptotagmin-1. We investigated these interactions using NMR and fluorescence spectroscopy. Synaptotagmin-1 binds to the SNARE complex through the polybasic and primary interfaces in solution. Ca<sup>2+</sup>-free synaptotagmin-1 binds to SNARE complexes anchored on PIP<sub>2</sub>-containing nanodiscs. R398Q/R399Q and E295A/Y338W mutations at the primary interface, which strongly impair neurotransmitter release, disrupt and enhance synaptotagmin-1-SNARE complex binding, respectively. Ca<sup>2+</sup> induces tight binding of synaptotagmin-1 to PIP<sub>2</sub>-containing nanodiscs, releasing synaptotagmin-1-SNARE interactions. Specific effects of mutations in the polybasic region on Ca<sup>2+</sup>-dependent synaptotagmin-1-PIP<sub>2</sub>-membrane interactions correlate with their effects on release. Our data suggest that synaptotagmin-1 binds to the SNARE complex through the primary interface and that Ca<sup>2+</sup> releases this interaction, inducing PIP<sub>2</sub>/membrane binding and allowing cooperation between synaptotagmin-1 and the SNAREs in membrane fusion to trigger release.</p>
NMR data in 'Ca2+-dependent release of Synaptotagmin-1 from the SNARE complex on phosphatidylinositol 4,5-bisphosphate-containing membranes' by Voleti, Jaczynska and Rizo, eLife 2020
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Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface
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Synaptotagmin 2 is ectopically overexpressed in a widely used CaMK2a-Cre mouse line [T29-1 dataset]
GEO Series GSE179802. Mus musculus. 8 samples. Type: Expression profiling by high throughput sequencing.
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