ArticleJournal of molecular biology2009
Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridging.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- The AD3 locus of synaptotagmin-1 C2 domains modulates domain stability.Biophysical journal · 2025Article
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- Impaired activity and membrane association of most calpain-5 mutants causal for neovascular inflammatory vitreoretinopathy.Biochimica et biophysica acta. Molecular basis of disease · 2023Article
- Review
- SNARE complex alters the interactions of the CaBiophysical journal · 2021Article
- Conserved arginine residues in synaptotagmin 1 regulate fusion pore expansion through membrane contact.Nature communications · 2021Article
- Conformational Differences Are Observed for the Active and Inactive Forms of Pinholin SThe journal of physical chemistry. B · 2020Article
- Membrane Association and Functional Mechanism of Synaptotagmin-1 in Triggering Vesicle Fusion.Biophysical journal · 2020Article
- Interference of pH buffer with PbMetallomics : integrated biometal science · 2020Article
- Phosphatidylinositol 4,5 Bisphosphate Controls the cis and trans Interactions of Synaptotagmin 1.Biophysical journal · 2019Article
- Membrane-Binding Cooperativity and Coinsertion by C2AB Tandem Domains of Synaptotagmins 1 and 7.Biophysical journal · 2019Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- Choice of reconstitution protocol modulates the aggregation state of full-length membrane-reconstituted synaptotagmin-1.Protein science : a publication of the Protein Society · 2018Article
- Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.Biophysical journal · 2017Article
- Differential Membrane Binding Mechanics of Synaptotagmin Isoforms Observed in Atomic Detail.Biochemistry · 2017Article
- PtdInsPeLife · 2016Article
- Membrane Docking of the Synaptotagmin 7 C2A Domain: Electron Paramagnetic Resonance Measurements Show Contributions from Two Membrane Binding Loops.Biochemistry · 2015Article
- Calcium binding promotes conformational flexibility of the neuronal Ca(2+) sensor synaptotagmin.Biophysical journal · 2015Article
- Reconstituting SNARE-mediated membrane fusion at the single liposome level.Methods in cell biology · 2015Article
- Lateral diffusion of proteins on supported lipid bilayers: additive friction of synaptotagmin 7 C2A-C2B tandem domains.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Synaptotagmin 1 (syt1) is a synaptic vesicle membrane protein that functions as the Ca(2)(+) sensor in neuronal exocytosis. Here, site-directed spin labeling was used to generate models for the solution and membrane-bound structures of a soluble fragment of syt1 containing its two C2 domains, C2A and C2B. In solution, distance restraints between the two C2 domains of syt1 were measured using double electron-electron resonance and used in a simulated annealing routine to generate models for the structure of the tandem C2A-C2B fragment. The data indicate that the two C2 domains are flexibly linked and do not interact with each other in solution, with or without Ca(2+). However, the favored orientation is one where the Ca(2+)-binding loops are oriented in opposite directions. A similar approach was taken for membrane-associated C2A-C2B, combining both distances and bilayer depth restraints with simulated annealing. The restraints can only be satisfied if the Ca(2+) and membrane-binding surfaces of the domains are oriented in opposite directions so that C2A and C2B are docked to opposing bilayers. The result suggests that syt1 functions to bridge across the vesicle and plasma membrane surfaces in a Ca(2+)-dependent manner.
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