ArticleJournal of molecular biology2011
Synaptotagmin 1 and SNAREs form a complex that is structurally heterogeneous.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Dynamic formation of the protein-lipid prefusion complex.Biophysical journal · 2024Article
- Dynamic Formation of the Protein-Lipid Pre-fusion Complex.bioRxiv : the preprint server for biology · 2024Article
- Review
- On the difficulties of characterizing weak protein interactions that are critical for neurotransmitter release.FEBS open bio · 2022Review
- SNARE complex alters the interactions of the CaBiophysical journal · 2021Article
- Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018Review
- The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018Article
- A Post-Docking Role of Synaptotagmin 1-C2B Domain Bottom Residues R398/399 in Mouse Chromaffin Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength.Nature structural & molecular biology · 2015Article
- Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution.Nature structural & molecular biology · 2015Article
- PI(4,5)P₂-binding effector proteins for vesicle exocytosis.Biochimica et biophysica acta · 2015Review
- Calcium binding promotes conformational flexibility of the neuronal Ca(2+) sensor synaptotagmin.Biophysical journal · 2015Article
- Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Scientific reports · 2015Article
- Control of membrane gaps by synaptotagmin-Ca2+ measured with a novel membrane distance ruler.Nature communications · 2014Article
- The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.The Journal of biological chemistry · 2014Article
- Automated structure refinement for a protein heterodimer complex using limited EPR spectroscopic data and a rigid-body docking algorithm: a three-dimensional model for an ankyrin-CDB3 complex.The journal of physical chemistry. B · 2014Article
- The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.Cellular and molecular life sciences : CMLS · 2014Review
- Synaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.Nature structural & molecular biology · 2013Article
- Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Synaptotagmin 1 (syt1) functions as a Ca(2+)-sensor for neuronal exocytosis. Here, site-directed spin labeling was used to examine the complex formed between a soluble fragment of syt1, which contains its two C2 domains, and the neuronal core soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex. Changes in electron paramagnetic resonance lineshape and accessibility for spin-labeled syt1 mutants indicate that in solution, the assembled core SNARE complex contacts syt1 in several regions. For the C2B domain, contact occurs in the polybasic face and sites opposite the Ca(2+)-binding loops. For the C2A domain, contact is seen with the SNARE complex in a region near loop 2. Double electron-electron resonance was used to estimate distances between the two C2 domains of syt1. These distances have broad distributions in solution, which do not significantly change when syt1 is fully associated with the core SNARE complex. The broad distance distributions indicate that syt1 is structurally heterogeneous when bound to the SNAREs and does not assume a well-defined structure. Simulated annealing using electron paramagnetic resonance-derived distance restraints produces a family of syt1 structures where the Ca(2+)-binding regions of each domain face in roughly opposite directions. The results suggest that when associated with the SNAREs, syt1 is configured to bind opposing bilayers, but that the syt1/SNARE complex samples multiple conformational states.
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