ArticleThe Journal of cell biology2000
The C2B domain of synaptotagmin is a Ca(2+)-sensing module essential for exocytosis.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 118 citations in OpenAlex.
- Quantitative single-molecule analysis of assembly and CaCommunications biology · 2024Article
- Simulations of active zone structure and function at mammalian NMJs predict that loss of calcium channels alone is not sufficient to replicate LEMS effects.Journal of neurophysiology · 2023Article
- Clinical and Pathologic Features of Congenital Myasthenic Syndromes Caused by 35 Genes-A Comprehensive Review.International journal of molecular sciences · 2023Review
- Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021Review
- Cerebrospinal Fluid Biomarkers of Alzheimer's Disease: Current Evidence and Future Perspectives.Brain sciences · 2021Review
- How Membrane Geometry Regulates Protein Sorting Independently of Mean Curvature.ACS central science · 2020Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- Article
- Different states of synaptotagmin regulate evoked versus spontaneous release.Nature communications · 2016Article
- Structural elements that underlie Doc2β function during asynchronous synaptic transmission.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Transmembrane tethering of synaptotagmin to synaptic vesicles controls multiple modes of neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The cytoplasmic domain of rat synaptotagmin I enhances synaptic transmission.Cellular and molecular neurobiology · 2014Article
- Linker mutations reveal the complexity of synaptotagmin 1 action during synaptic transmission.Nature neuroscience · 2014Article
- Article
- Genetic analysis of synaptotagmin C2 domain specificity in regulating spontaneous and evoked neurotransmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- All three components of the neuronal SNARE complex contribute to secretory vesicle docking.The Journal of cell biology · 2012Article
- Ca2+ regulates the Drosophila Stoned-A and Stoned-B proteins interaction with the C2B domain of Synaptotagmin-1.PloS one · 2012Article
- Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion.The Journal of cell biology · 2011Article
- Interaction of synaptotagmin with lipid bilayers, analyzed by single-molecule force spectroscopy.Biophysical journal · 2010Article
- Differential regulation of synchronous versus asynchronous neurotransmitter release by the C2 domains of synaptotagmin 1.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
The synaptic vesicle protein synaptotagmin I has been proposed to serve as a Ca(2+) sensor for rapid exocytosis. Synaptotagmin spans the vesicle membrane once and possesses a large cytoplasmic domain that contains two C2 domains, C2A and C2B. Multiple Ca(2+) ions bind to the membrane proximal C2A domain. However, it is not known whether the C2B domain also functions as a Ca(2+)-sensing module. Here, we report that Ca(2+) drives conformational changes in the C2B domain of synaptotagmin and triggers the homo- and hetero-oligomerization of multiple isoforms of the protein. These effects of Ca(2)+ are mediated by a set of conserved acidic Ca(2)+ ligands within C2B; neutralization of these residues results in constitutive clustering activity. We addressed the function of oligomerization using a dominant negative approach. Two distinct reagents that block synaptotagmin clustering potently inhibited secretion from semi-intact PC12 cells. Together, these data indicate that the Ca(2)+-driven clustering of the C2B domain of synaptotagmin is an essential step in excitation-secretion coupling. We propose that clustering may regulate the opening or dilation of the exocytotic fusion pore.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.