The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
synaptotagmin Mutants Reveal Essential Functions for the C2B Domain in Ca2+-Triggered Fusion and Recycling of Synaptic Vesicles In Vivo
Open accessAbstract
Synaptotagmin has been proposed to function as a Ca(2+) sensor that regulates synaptic vesicle exocytosis, whereas the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex is thought to form the core of a conserved membrane fusion machine. Little is known concerning the functional relationships between synaptotagmin and SNAREs. Here we report that synaptotagmin can facilitate SNARE complex formation in vitro and that synaptotagmin mutations disrupt SNARE complex formation in vivo. Synaptotagmin oligomers efficiently bind SNARE complexes, whereas Ca(2+) acting via synaptotagmin triggers cross-linking of SNARE complexes into dimers. Mutations in Drosophila that delete the C2B domain of synaptotagmin disrupt clathrin AP-2 binding and endocytosis. In contrast, a mutation that blocks Ca(2+)-triggered conformational changes in C2B and diminishes Ca(2+)-triggered synaptotagmin oligomerization results in a postdocking defect in neurotransmitter release and a decrease in SNARE assembly in vivo. These data suggest that Ca(2+)-driven oligomerization via the C2B domain of synaptotagmin may trigger synaptic vesicle fusion via the assembly and clustering of SNARE complexes.
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Cites
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417 · cited 5×
“We note that in some experiments, Ca21 alone was able to trigger low levels of cross-linked dimer formation, perhaps via direct effects on the SNARE complex (Sutton et al., 1998).”
BackgroundResultInfluentialSynaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse
Geppert, M., Goda, Y., Hammer, R. E., Li, C., Rosahl, T. W., Stevens, C. F., & Südhof, T. C. (1994) · Cell · doi:10.1016/0092-8674(94)90556-8 · Cited by 1,483
McBride, H. M., Rybin, V., Murphy, C., Giner, A., Teasdale, R., & Zerial, M. (1999) · Cell · doi:10.1016/s0092-8674(00)81966-2 · Cited by 520
Cited by
Synaptotagmin: A Ca2+ sensor that triggers exocytosis?
Chapman, E. R. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm855 · Cited by 485
Self-citationThe C2B Ca2+-binding motif of synaptotagmin is required for synaptic transmission in vivo
Mackler, J. M., Drummond, J. A., Loewen, C. A., Robinson, I. M., & Reist, N. E. (2002) · Nature · doi:10.1038/nature00846 · Cited by 323
Clathrin-mediated endocytosis: membrane factors pull the trigger
Takei, K., & Haucke, V. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02082-7 · Cited by 311
Synaptotagmin I Functions as a Calcium Sensor to Synchronize Neurotransmitter Release
Yoshihara, M., & Littleton, J. T. (2002) · Neuron · doi:10.1016/s0896-6273(02)01065-6 · Cited by 285
Self-citationSV2 modulates the size of the readily releasable pool of secretory vesicles
Xu, T., & Bajjalieh, S. M. (2001) · Nature Cell Biology · doi:10.1038/35087000 · Cited by 212
Metadata
- Authors
- Littleton, J. T., Bai, J., Vyas, B., Desai, R., Baltus, A. E., Garment, M. B., Carlson, S. D., Ganetzky, B., & Chapman, E. R.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2001-03-01
- Volume
- 21
- Issue
- 5
- Pages
- 1421-1433
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W1784572511
- Cited by
- 171
- References
- 3
- FWCI
- 8.19
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Littleton, J. T., Bai, J., Vyas, B., Desai, R., Baltus, A. E., Garment, M. B., Carlson, S. D., Ganetzky, B., & Chapman, E. R. (2001). synaptotagmin Mutants Reveal Essential Functions for the C2B Domain in Ca2+-Triggered Fusion and Recycling of Synaptic Vesicles In Vivo. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.21-05-01421.2001
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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