ArticleThe Journal of cell biology1999
Crystal structure of the cytosolic C2A-C2B domains of synaptotagmin III. Implications for Ca(+2)-independent snare complex interaction.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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65 citing papers in PubMed, 174 citations in OpenAlex.
- Role of calcium-sensor proteins in cell membrane repair.Bioscience reports · 2023Review
- Calcium Sensors of Neurotransmitter Release.Advances in neurobiology · 2023Article
- Article
- On the difficulties of characterizing weak protein interactions that are critical for neurotransmitter release.FEBS open bio · 2022Review
- Expression and distribution of synaptotagmin family members in the zebrafish retina.The Journal of comparative neurology · 2022Article
- Potential roles of synaptotagmin family members in cancers: Recent advances and prospects.Frontiers in medicine · 2022Review
- The C2A domain of synaptotagmin is an essential component of the calcium sensor for synaptic transmission.PloS one · 2020Article
- A mutually induced conformational fit underlies CaThe Journal of biological chemistry · 2019Article
- Exceptionally tight membrane-binding may explain the key role of the synaptotagmin-7 CProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Drosophila studies support a role for a presynaptic synaptotagmin mutation in a human congenital myasthenic syndrome.PloS one · 2017Article
- Different states of synaptotagmin regulate evoked versus spontaneous release.Nature communications · 2016Article
- Functional analysis of the interface between the tandem C2 domains of synaptotagmin-1.Molecular biology of the cell · 2016Article
- Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex.Nature communications · 2015Article
- From deep TLS validation to ensembles of atomic models built from elemental motions.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Linker mutations reveal the complexity of synaptotagmin 1 action during synaptic transmission.Nature neuroscience · 2014Article
- Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2.Structure (London, England : 1993) · 2014Article
- Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin.Biophysical journal · 2014Article
- Genetic analysis of synaptotagmin C2 domain specificity in regulating spontaneous and evoked neurotransmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Annexin A7 and SNAP23 interactions in alveolar type II cells and in vitro: a role for Ca(2+) and PKC.Biochimica et biophysica acta · 2012Article
- Towards automated crystallographic structure refinement with phenix.refine.Acta crystallographica. Section D, Biological crystallography · 2012Article
5 more citing papers are in PubMed but not listed here.
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3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Synaptotagmins are synaptic vesicle-associated, phospholipid-binding proteins most commonly associated with Ca(+2)-dependent exocytotic and Ca(+2)- independent endocytotic events. Synaptotagmin III is a 63.2-kD member of the synaptotagmin homology group; one of its characteristic properties is the ability to bind divalent cations and accessory proteins promiscuously. In the cytosolic portion of this protein, a flexible seven-amino acid linker joins two homologous C2 domains. The C2A domain binds to phospholipid membranes and other accessory proteins in a divalent cation-dependent fashion. The C2B domain promotes binding to other C2B domains, as well as accessory proteins independent of divalent cations. The 3.2 A crystal structure of synaptotagmin III, residues 295-566, which includes the C2A and C2B domains, exhibits differences in the shape of the Ca(+2)-binding pocket, the electrostatic surface potential, and the stoichiometry of bound divalent cations for the two domains. These observations may explain the disparate binding properties of the two domains. The C2A and the C2B domains do not interact; synaptotagmin, therefore, covalently links two independent C2 domains, each with potentially different binding partners. A model of synaptotagmin's involvement in Ca(+2)-dependent regulation of membrane fusion through its interaction with the SNARE complex is presented.
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