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A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding.
Open accessAbstract
Synaptotagmin I is a Ca(2+)- and phospholipid-binding protein of synaptic vesicles with an essential function in neurotransmission. Ca2+/phospholipid binding by synaptotagmin I may be mediated by its C2 domains, sequence motifs that have been implicated in the Ca2+ regulation of a variety of proteins. However, it is currently unknown if C2 domains are sufficient for Ca2+/phospholipid binding or if they even directly participate in Ca2+/phospholipid binding. In order to address this question, we have studied the Ca2+/phospholipid-binding properties of the first C2 domain of synaptotagmin I. Our results show that this C2 domain by itself binds Ca2+ and phospholipids with high affinity (half-maximal binding at 4-6 microM free Ca2+) and exhibits strong positive cooperativity. The C2 domain is specific for negatively charged phospholipids and for those divalent cations that are known to stimulate synaptic vesicle exocytosis (Ca2+ > Sr2+, Ba2+ >>> Mg2+). These studies establish that C2 domains can serve as independently folding Ca2+/phospholipid-binding domains. Furthermore, the cation specificity and the cooperativity of Ca2+ binding by the C2 domain from synaptotagmin I support a role for this protein in mediating the Ca2+ signal in neurotransmitter release.
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“Syt1 binds in a Ca2+-dependent manner to anionic membranes; during binding, anionic phospholipids and synaptotagmin C2 domains together coordinate calcium14–17.”
From Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis (2015) · cites this paper as [14]
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Metadata
- Authors
- Davletov, B. A., & Südhof, T. C.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-12
- Volume
- 268
- Issue
- 35
- Pages
- 26386-26390
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1591133722
- Cited by
- 480
- References
- 0
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 12 · 2021: 5 · 2020: 4 · 2019: 8 · 2018: 9 · 2017: 6 · 2016: 6 · 2015: 12 · 2014: 21 · 2013: 11 · 2012: 9
- FWCI
- 9.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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 › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- synaptotagmin-1, C2 domain, calcium binding, phospholipid binding, cooperative binding, synaptic vesicle exocytosis, neurotransmitter release, synaptic vesicles, protein folding
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Calcium, Calcium-Binding Proteins, Carbon, Enzyme Activation, Membrane Glycoproteins, Molecular Sequence Data, Nerve Tissue Proteins, Phospholipids, Protein Kinase C, DNA Primers, Synaptotagmins, Synaptotagmin I, Rats
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