Cited by 1,483Cellular transport and secretionNeuroscience and Neuropharmacology ResearchCalcium signaling and nucleotide metabolism

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Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse

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Geppert, Martin, Goda, Yukiko, Hammer, Robert E., Li, Cai, Rosahl, Thomas W., Stevens, Charles F., Südhof, Thomas C.·1994·Cell

DOI 10.1016/0092-8674(94)90556-8

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Abstract

Mice carrying a mutation in the synaptotagmin I gene were generated by homologous recombination. Mutant mice are phenotypically normal as heterozygotes, but die within 48 hr after birth as homozygotes. Studies of hippocampal neurons cultured from homozygous mutant mice reveal that synaptic transmission is severely impaired. The synchronous, fast component of Ca(2+)-dependent neurotransmitter release is decreased, whereas asynchronous release processes, including spontaneous synaptic activity (miniature excitatory postsynaptic current frequency) and release triggered by hypertonic solution or alpha-latrotoxin, are unaffected. Our findings demonstrate that synaptotagmin I function is required for Ca2+ triggering of synchronous neurotransmitter release, but is not essential for asynchronous or Ca(2+)-independent release. We propose that synaptotagmin I is the major low affinity Ca2+ sensor mediating Ca2+ regulation of synchronous neurotransmitter release in hippocampal neurons.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
SNAP receptors implicated in vesicle targeting and fusion
Söllner, T. H., Whiteheart, S. W., Brunner, M., Erdjument‐Bromage, H., Geromanos, S. J., Tempst, P., & Rothman, J. E. (1993) · Nature · doi:10.1038/362318a0 · Cited by 3,239
Site-directed mutagenesis by gene targeting in mouse embryo-derived stem cells
Thomas, K. R., & Capecchi, M. R. (1987) · Cell · doi:10.1016/0092-8674(87)90646-5 · Cited by 2,355
Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
Soriano, P. M., Montgomery, C. A., Geske, R. S., & Bradley, A. (1991) · Cell · doi:10.1016/0092-8674(91)90499-o · Cited by 1,997
Spontaneous subthreshold activity at motor nerve endings
Fatt, P., & Katz, B. (1952) · The Journal of Physiology · doi:10.1113/jphysiol.1952.sp004735 · Cited by 1,835
Co‐operative action of calcium ions in transmitter release at the neuromuscular junction
Dodge, F. A., & Rahamimoff, R. (1967) · The Journal of Physiology · doi:10.1113/jphysiol.1967.sp008367 · Cited by 1,315
Syntaxin: A Synaptic Protein Implicated in Docking of Synaptic Vesicles at Presynaptic Active Zones
Bennett, M. K., Calakos, N., & Scheller, R. H. (1992) · Science · doi:10.1126/science.1321498 · Cited by 1,263
Synaptotagmin: a Calcium Sensor on the Synaptic Vesicle Surface
Brose, N., Petrenko, A. G., Südhof, T. C., & Jahn, R. (1992) · Science · doi:10.1126/science.1589771 · Cited by 979
Self-citation

Show all 45 references

Research works printed but not linked: 1

Shirataki, 1993, Rabphillin-3A, a putative target protein for smg p25Arab3A small GTP-binding protein related to synaptotagmin, Mol. Cell. Biol., 13, 2061, 10.1128/MCB.13.4.2061 · DOI

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Self-citation
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Beleboni, R. O., Pizzo, A. B., Fontana, A. C. K., Carolino, R. O. G., Coutinho‐Netto, J., & dos Santos, W. F. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.03.049 · Cited by 74
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Kohli, B. M., Pflieger, D., Mueller, L. N., Carbonetti, G., Aebersold, R. H., Nitsch, R. M., & Konietzko, U. (2012) · Journal of Proteome Research · doi:10.1021/pr300123g · Cited by 77
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Lynch, K. L., Gerona, R. R. L., Larsen, E. C., Marcia, R., Mitchell, J. C., & Martin, T. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0368 · Cited by 79
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Self-citation
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Self-citation
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Self-citation
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Self-citation
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Pyle, R. A., Schivell, A. E., Hidaka, H., & Bajjalieh, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000674200 · Cited by 70
Dynamics of dendritic calcium transients evoked by quantal release at excitatory hippocampal synapses
Murthy, V. N., Sejnowski, T. J., & Stevens, C. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.901 · Cited by 70
Self-citation
Structure of the Janus-faced C2B domain of rabphilin
Ubach, J., Garcia, J. M., Nittler, M., Südhof, T., & Rizo, J. (1999) · Nature Cell Biology · doi:10.1038/10076 · Cited by 72
Self-citation
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Cho, R. W., Kümmel, D., Li, F., Baguley, S. W., Coleman, J., Rothman, J. E., & Littleton, J. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1409311111 · Cited by 69
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Williams, C. L., & Smith, S. M. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24116 · Cited by 71
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Authors: Geppert, M., Goda, Y., Hammer, R. E., Li, C., Rosahl, T. W., Stevens, C. F., & Südhof, T. C.
Affiliations: The University of Texas Southwestern Medical Center (US)
Salk Institute for Biological Studies (US)
Howard Hughes Medical Institute (US)
ORCID: Goda, Yukiko
Rosahl, Thomas W.
Stevens, Charles F.
Südhof, Thomas C.
Venue: Cell
Publisher: Elsevier BV
Published: 1994-11
Volume: 79
Issue: 4
Pages: 717-727
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(94)90556-8
OpenAlex: W2165302477
Cited by: 1,483
References: 45
Citations by year: 2026: 17 · 2025: 24 · 2024: 34 · 2023: 36 · 2022: 41 · 2021: 42 · 2020: 47 · 2019: 49 · 2018: 43 · 2017: 41 · 2016: 31 · 2015: 41 · 2014: 51 · 2013: 33 · 2012: 59
FWCI: 20.67
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft
National Institutes of Health (5r01ns012961-22)
National Institute of Neurological Disorders and Stroke (R0 NS 12961-17)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords: synaptotagmin-1, calcium sensor, asynchronous release, calcium-independent release, hippocampal neurons, synaptic transmission, mouse mutants, alpha-latrotoxin, spontaneous synaptic activity
MeSH terms: Animals, Animals, Newborn, Base Sequence, Brain, Calcium, Calcium-Binding Proteins, Exons, Hippocampus, Homozygote, Hypertonic Solutions, Membrane Glycoproteins, Mice, Neurologic Mutants, Molecular Sequence Data, Mutation, Nerve Tissue Proteins, Synaptic Transmission, Neurons, Reference Values, Spider Venoms, Synapses, Restriction Mapping, Polymerase Chain Reaction, Mutagenesis, DNA Primers, Neurotransmitter Agents, Synaptotagmins, Synaptotagmin I, Mice

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Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse

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