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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-10737 | |||||||||
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Title | Actin filament structure from vinculin-induced bundles | |||||||||
![]() | Actin filament structure from vinculin-induced bundles | |||||||||
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Biological species | ![]() ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 14.2 Å | |||||||||
![]() | Boujemaa-Paterski R / Martins B / Eibauer M / Geiger B / Medalia O | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Talin-activated vinculin interacts with branched actin networks to initiate bundles. Authors: Rajaa Boujemaa-Paterski / Bruno Martins / Matthias Eibauer / Charlie T Beales / Benjamin Geiger / Ohad Medalia / ![]() ![]() ![]() Abstract: Vinculin plays a fundamental role in integrin-mediated cell adhesion. Activated by talin, it interacts with diverse adhesome components, enabling mechanical coupling between the actin cytoskeleton ...Vinculin plays a fundamental role in integrin-mediated cell adhesion. Activated by talin, it interacts with diverse adhesome components, enabling mechanical coupling between the actin cytoskeleton and the extracellular matrix. Here we studied the interactions of activated full-length vinculin with actin and the way it regulates the organization and dynamics of the Arp2/3 complex-mediated branched actin network. Through a combination of surface patterning and light microscopy experiments we show that vinculin can bundle dendritic actin networks through rapid binding and filament crosslinking. We show that vinculin promotes stable but flexible actin bundles having a mixed-polarity organization, as confirmed by cryo-electron tomography. Adhesion-like synthetic design of vinculin activation by surface-bound talin revealed that clustered vinculin can initiate and immobilize bundles from mobile Arp2/3-branched networks. Our results provide a molecular basis for coordinate actin bundle formation at nascent adhesions. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 8.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.4 KB 11.4 KB | Display Display | ![]() |
Images | ![]() | 29 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 204.1 KB | Display | ![]() |
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Full document | ![]() | 203.2 KB | Display | |
Data in XML | ![]() | 5.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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EM raw data | ![]() Data size: 4.0 Data #1: Tomograms of actin bundles induced by full length vinculin [tilt series]) |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Actin filament structure from vinculin-induced bundles | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 3.443 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Actin
Entire | Name: Actin |
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Components |
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-Supramolecule #1: Actin
Supramolecule | Name: Actin / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Actin
Macromolecule | Name: Actin / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTL KYPIEHGIIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE K MTQIMFET FNVPAMYVAI QAVLSLYASG RTTGIVLDSG DGVTHNVPIY ...String: MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTL KYPIEHGIIT NWDDMEKIWH HTFYNELRVA PEEHPTLLTE APLNPKANRE K MTQIMFET FNVPAMYVAI QAVLSLYASG RTTGIVLDSG DGVTHNVPIY EGYALPHAIM RL DLAGRDL TDYLMKILTE RGYSFVTTAE REIVRDIKEK LCYVALDFEN EMATAASSSS LEK SYELPD GQVITIGNER FRCPETLFQP SFIGMESAGI HETTYNSIMK CDIDIRKDLY ANNV MSGGT TMYPGIADRM QKEITALAPS TMKIKIIAPP ERKYSVWIGG SILASLSTFQ QMWIT KQEY DEAGPSIVHR KCF |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Concentration | 0.4 mg/mL |
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Buffer | pH: 7.8 |
Grid | Model: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 1.2 sec. / Average electron dose: 1.1 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Calibrated magnification: 42000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 4.5 µm / Nominal defocus min: 3.5 µm / Nominal magnification: 14522 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |