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Cited by 480Cellular transport and secretionNeuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase Signaling

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A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding.

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Davletov, B A, Südhof, T C·1993·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)74326-9
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Abstract

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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Metadata

Authors
Davletov, B. A., & Südhof, T. C.
Affiliations
Howard Hughes Medical Institute (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-12
Volume
268
Issue
35
Pages
26386-26390
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)74326-9
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
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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