The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Molecular machines governing exocytosis of synaptic vesicles
Open accessAbstract
Calcium-dependent exocytosis of synaptic vesicles mediates the release of neurotransmitters. Important proteins in this process have been identified such as the SNAREs, synaptotagmins, complexins, Munc18 and Munc13. Structural and functional studies have yielded a wealth of information about the physiological role of these proteins. However, it has been surprisingly difficult to arrive at a unified picture of the molecular sequence of events from vesicle docking to calcium-triggered membrane fusion. Using mainly a biochemical and biophysical perspective, we briefly survey the molecular mechanisms in an attempt to functionally integrate the key proteins into the emerging picture of the neuronal fusion machine.
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Cites
Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,547
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 1×
“A tight bundle of four parallel a-helices is formed, each contributed by a different SNARE motif (17,18), which progresses towards the C-terminal membrane anchors (‘zippering’), thus pulling the membranes tightly together (19).”
BackgroundSelf-citationMembrane Fusion: Grappling with SNARE and SM Proteins
Südhof, T. C., & Rothman, J. E. (2009) · Science · doi:10.1126/science.1161748 · Cited by 2,027
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · cited 1×
“This helps to explain why unrelated classes of fusion proteins evolved in parallel to the SNAREs, such as those fusing cells (95), viruses (96), mitochondria (97) or the endoplasmic reticulum (98).”
BackgroundMunc13 mediates the transition from the closed syntaxin–Munc18 complex to the SNARE complex
Ma, C., Li, W., Xu, Y., & Rizo, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2047 · Cited by 363
Conformational switch of syntaxin-1 controls synaptic vesicle fusion
Gerber, S. H., Rah, J.-C., Min, S.-W., Liu, X., de Wit, H., Dulubova, I., Meyer, A. C., Rizo, J., Arancillo, M., Hammer, R. E., et al. (2008) · Science · doi:10.1126/science.1163174 · Cited by 294
Margittai, M., Widengren, J., Schweinberger, E., Schröder, G. F., Felekyan, S., Haustein, E., König, M., Fasshauer, D., Grubmüller, H., Jahn, R., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2331232100 · Cited by 290
Self-citationAraç, D., Chen, X., Khant, H. A., Ubach, J., Ludtke, S. J., Kikkawa, M., Johnson, A. E., Chiu, W., Südhof, T. C., & Rizo, J. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1056 · Cited by 256
The Janus-faced nature of the C2B domain is fundamental for synaptotagmin-1 function
Xue, M., Ma, C., Craig, T. K., Rosenmund, C., & Rizo, J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1508 · Cited by 131
Dynamic Ca 2+ -Dependent Stimulation of Vesicle Fusion by Membrane-Anchored Synaptotagmin 1
Lee, H.-K., Yang, Y., Su, Z., Hyeon, C., Lee, T.-S., Lee, H.-W., Kweon, D.-H., Shin, Y.-K., & Yoon, T.-Y. (2010) · Science · doi:10.1126/science.1187722 · Cited by 123
Cited by
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
Neurotransmitter Release: The Last Millisecond in the Life of a Synaptic Vesicle
Südhof, T. C. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.022 · Cited by 1,197
Biomarkers for Alzheimer's disease: current status and prospects for the future
Blennow, K., & Zetterberg, H. (2018) · Journal of Internal Medicine · doi:10.1111/joim.12816 · Cited by 1,000
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins
Wilhelm, B. G., Mandad, S., Truckenbrodt, S., Kröhnert, K., Schäfer, C., Rammner, B., Koo, S. J., Claßen, G. A., Krauss, M., Haucke, V., et al. (2014) · Science · doi:10.1126/science.1252884 · Cited by 770
The mechanisms and functions of synaptic facilitation.
Jackman, S. L., & Regehr, W. G. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.047 · Cited by 489
Metadata
- Authors
- Jahn, R., & Fasshauer, D.
- Venue
- Nature
- Published
- 2012-10
- Volume
- 490
- Issue
- 7419
- Pages
- 201-207
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2048465987
- Cited by
- 970
- References
- 11
- FWCI
- 38.28
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
