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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Short (SNARE complex dependent) synaptic vesicle tether | |||||||||
Map data | Short tether average | |||||||||
Sample |
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Keywords | SNARE complex Presynaptic Synaptic vesicle tether Active zone complex Vesicle fusion Synaptic transmission / EXOCYTOSIS | |||||||||
| Biological species | ![]() | |||||||||
| Method | subtomogram averaging / cryo EM / Resolution: 31.2 Å | |||||||||
Authors | Lucic V / Oroczo-Borunda DH | |||||||||
| Funding support | France, 1 items
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Citation | Journal: Sci Adv / Year: 2023Title: Munc13- and SNAP25-dependent molecular bridges play a key role in synaptic vesicle priming. Authors: Christos Papantoniou / Ulrike Laugks / Julia Betzin / Cristina Capitanio / José Javier Ferrero / José Sánchez-Prieto / Susanne Schoch / Nils Brose / Wolfgang Baumeister / Benjamin H ...Authors: Christos Papantoniou / Ulrike Laugks / Julia Betzin / Cristina Capitanio / José Javier Ferrero / José Sánchez-Prieto / Susanne Schoch / Nils Brose / Wolfgang Baumeister / Benjamin H Cooper / Cordelia Imig / Vladan Lučić / ![]() Abstract: Synaptic vesicle tethering, priming, and neurotransmitter release require a coordinated action of multiple protein complexes. While physiological experiments, interaction data, and structural studies ...Synaptic vesicle tethering, priming, and neurotransmitter release require a coordinated action of multiple protein complexes. While physiological experiments, interaction data, and structural studies of purified systems were essential for our understanding of the function of the individual complexes involved, they cannot resolve how the actions of individual complexes integrate. We used cryo-electron tomography to simultaneously image multiple presynaptic protein complexes and lipids at molecular resolution in their native composition, conformation, and environment. Our detailed morphological characterization suggests that sequential synaptic vesicle states precede neurotransmitter release, where Munc13-comprising bridges localize vesicles <10 nanometers and soluble -ethylmaleimide-sensitive factor attachment protein 25-comprising bridges <5 nanometers from the plasma membrane, the latter constituting a molecularly primed state. Munc13 activation supports the transition to the primed state via vesicle bridges to plasma membrane (tethers), while protein kinase C promotes the same transition by reducing vesicle interlinking. These findings exemplify a cellular function performed by an extended assembly comprising multiple molecularly diverse complexes. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_52342.map.gz | 71.3 KB | EMDB map data format | |
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| Header (meta data) | emd-52342-v30.xml emd-52342.xml | 23.7 KB 23.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_52342_fsc.xml | 2.4 KB | Display | FSC data file |
| Images | emd_52342.png | 47.3 KB | ||
| Masks | emd_52342_msk_1.map | 1 MB | Mask map | |
| Filedesc metadata | emd-52342.cif.gz | 5.9 KB | ||
| Others | emd_52342_additional_1.map.gz emd_52342_half_map_1.map.gz emd_52342_half_map_2.map.gz | 57.8 KB 739.7 KB 738.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-52342 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-52342 | HTTPS FTP |
-Validation report
| Summary document | emd_52342_validation.pdf.gz | 570.1 KB | Display | EMDB validaton report |
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| Full document | emd_52342_full_validation.pdf.gz | 569.6 KB | Display | |
| Data in XML | emd_52342_validation.xml.gz | 7.3 KB | Display | |
| Data in CIF | emd_52342_validation.cif.gz | 9.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52342 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-52342 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_52342.map.gz / Format: CCP4 / Size: 1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Short tether average | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 8.78 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_52342_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: Short tether average without synaptic vesicle and plasma...
| File | emd_52342_additional_1.map | ||||||||||||
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| Annotation | Short tether average without synaptic vesicle and plasma membrane contributions | ||||||||||||
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-Half map: Half 1
| File | emd_52342_half_map_1.map | ||||||||||||
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| Annotation | Half 1 | ||||||||||||
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-Half map: Half 2
| File | emd_52342_half_map_2.map | ||||||||||||
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| Annotation | Half 2 | ||||||||||||
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Sample components
-Entire : Synaptosome
| Entire | Name: Synaptosome |
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| Components |
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-Supramolecule #1: Synaptosome
| Supramolecule | Name: Synaptosome / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all / Details: Synaptosomal fraction from rodent Hippocampus |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 132 KDa |
-Macromolecule #1: Putative neuronal SNARE complex (Syntaxin-1, SNAP25, Synaptobrevi...
| Macromolecule | Name: Putative neuronal SNARE complex (Syntaxin-1, SNAP25, Synaptobrevin-2) with Complexin-1 and Synptotagmin-1 type: other / ID: 1 Details: Native, endogenous mammalian protein complex. Likely composed of neuronal SNARE complex (Syntaxin-1, SNAP25, Synaptobrevin-2) with Complexin-1 and Synptotagmin-1 Classification: other |
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| Source (natural) | Organism: ![]() |
| Sequence | String: MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | subtomogram averaging |
| Aggregation state | cell |
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Sample preparation
| Concentration | 0.4 mg/mL |
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| Buffer | pH: 7.4 / Component - Concentration: 300.0 mM / Component - Formula: HBM / Component - Name: Hepes-buffered medium Details: 140 mM NaCl, 5 mM KCl, 5mM NaHCO3, 1.2 mM NaH2PO4-H2O, 1 mM MgCl26-H2O, 10 mM Glucose, 10 mM Hepes, 1.2 mM CaCl2 |
| Grid | Model: Quantifoil R2/1 / Material: GOLD / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 120 sec. |
| Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER Details: Portable manual plunger made at Max Planck Institute of Biochemistry. |
| Details | Synaptosomal fraction (P2) was obtained from DIV 28-30 hippocampal organotypic slices. |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Phase plate: VOLTA PHASE PLATE / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 1.5 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.0 µm / Nominal defocus min: 0.5 µm |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
France, 1 items
Citation




Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN

