ArticleMolecular biology of the cell2006
C2B polylysine motif of synaptotagmin facilitates a Ca2+-independent stage of synaptic vesicle priming in vivo.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Disease-causing mutations in Synaptotagmin can act via dominant-negative, gain-of-function or haploinsufficient mechanisms.bioRxiv : the preprint server for biology · 2026Article
- Synergistic regulation of fusion pore opening and dilation by SNARE and synaptotagmin-1.Journal of molecular cell biology · 2024Article
- Calcium Sensors of Neurotransmitter Release.Advances in neurobiology · 2023Article
- Polybasic Patches in Both C2 Domains of Synaptotagmin-1 Are Required for Evoked Neurotransmitter Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Synaptotagmin-1 is a bidirectional CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Lysine acetylation regulates the interaction between proteins and membranes.Nature communications · 2021Article
- Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021Review
- Dynamics of Neuromuscular Transmission Reproduced by Calcium-Dependent and Reversible Serial Transitions in the Vesicle Fusion Complex.Frontiers in synaptic neuroscience · 2021Article
- Synaptotagmin-1 membrane binding is driven by the C2B domain and assisted cooperatively by the C2A domain.Scientific reports · 2020Article
- The C2A domain of synaptotagmin is an essential component of the calcium sensor for synaptic transmission.PloS one · 2020Article
- Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin.Nature communications · 2019Article
- Synaptotagmin oligomerization is essential for calcium control of regulated exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Productive and Non-productive Pathways for Synaptotagmin 1 to Support CaFrontiers in molecular neuroscience · 2017Article
- Complexins: small but capable.Cellular and molecular life sciences : CMLS · 2015Review
- A Post-Docking Role of Synaptotagmin 1-C2B Domain Bottom Residues R398/399 in Mouse Chromaffin Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- PI(4,5)P₂-binding effector proteins for vesicle exocytosis.Biochimica et biophysica acta · 2015Review
- Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Scientific reports · 2015Article
- Synaptotagmin 1 and Ca2+ drive trans SNARE zippering.Scientific reports · 2014Article
- Complexin arrests a pool of docked vesicles for fast Ca2+-dependent release.The EMBO journal · 2012Article
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4 authors.
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Abstract
Synaptotagmin I, a synaptic vesicle protein required for efficient synaptic transmission, contains a highly conserved polylysine motif necessary for function. Using Drosophila, we examined in which step of the synaptic vesicle cycle this motif functions. Polylysine motif mutants exhibited an apparent decreased Ca2+ affinity of release, and, at low Ca2+, an increased failure rate, increased facilitation, and increased augmentation, indicative of a decreased release probability. Disruption of Ca2+ binding, however, cannot account for all of the deficits in the mutants; rather, the decreased release probability is probably due to a disruption in the coupling of synaptotagmin to the release machinery. Mutants exhibited a major slowing of recovery from synaptic depression, which suggests that membrane trafficking before fusion is disrupted. The disrupted process is not endocytosis because the rate of FM 1-43 uptake was unchanged in the mutants, and the polylysine motif mutant synaptotagmin was able to rescue the synaptic vesicle depletion normally found in syt(null) mutants. Thus, the polylysine motif functions after endocytosis and before fusion. Finally, mutation of the polylysine motif inhibits the Ca2+-independent ability of synaptotagmin to accelerate SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor)-mediated fusion. Together, our results demonstrate that the polylysine motif is required for efficient Ca2+-independent docking and/or priming of synaptic vesicles in vivo.
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