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- EMDB-50814: Real space helical reconstruction of cofilin actin in the microtu... -
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Open data
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Basic information
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Title | Real space helical reconstruction of cofilin actin in the microtubule lumen of human platelets | |||||||||||||||||||||||||||||||||||||||
![]() | Real space helical reconstruction of cofilin actin in the microtubule lumen of human platelets | |||||||||||||||||||||||||||||||||||||||
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![]() | cofilin / actin / filament / CYTOSOLIC PROTEIN | |||||||||||||||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 20.0 Å | |||||||||||||||||||||||||||||||||||||||
![]() | Tsuji C / Bradshaw M / Paul DM / Dodding MP | |||||||||||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: CryoET reveals actin filaments within platelet microtubules. Authors: Chisato Tsuji / Marston Bradshaw / Megan F Allen / Molly L Jackson / Judith Mantell / Ufuk Borucu / Alastair W Poole / Paul Verkade / Ingeborg Hers / Danielle M Paul / Mark P Dodding / ![]() Abstract: Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure ...Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure where F-actin occupies the microtubule lumen. Whether these cytoskeletal hybrids exist in physiological settings and how they are formed is unclear. Here, we show that the short-crossover Class I actin filament previously identified inside microtubules in human HAP1 cells is cofilin-bound F-actin. Lumenal F-actin can be reconstituted in vitro, but cofilin is not essential. Moreover, actin filaments with both cofilin-bound and canonical morphologies reside within human platelet microtubules under physiological conditions. We propose that stress placed upon the microtubule network during motor-driven microtubule looping and sliding may facilitate the incorporation of actin into microtubules. | |||||||||||||||||||||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 760.4 KB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.2 KB 11.2 KB | Display Display | ![]() |
Images | ![]() | 29.4 KB | ||
Filedesc metadata | ![]() | 4.1 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 317.8 KB | Display | ![]() |
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Full document | ![]() | 317.4 KB | Display | |
Data in XML | ![]() | 4.7 KB | Display | |
Data in CIF | ![]() | 5.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Real space helical reconstruction of cofilin actin in the microtubule lumen of human platelets | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 3.75 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Cofilin bound actin structure found in the lumen of microtubules ...
Entire | Name: Cofilin bound actin structure found in the lumen of microtubules in human platelets |
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Components |
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-Supramolecule #1: Cofilin bound actin structure found in the lumen of microtubules ...
Supramolecule | Name: Cofilin bound actin structure found in the lumen of microtubules in human platelets type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 7.3 |
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Vitrification | Cryogen name: ETHANE / Instrument: LEICA EM GP |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 3.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 7.0 µm / Nominal defocus min: 3.0 µm / Nominal magnification: 53000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 27.5 Å Applied symmetry - Helical parameters - Δ&Phi: 162 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 20.0 Å / Resolution method: OTHER Details: A sub-volume containing the filament was extracted from a tomogram, which was then 2D projected. The projected image was used for real space helical reconstruction to create the map. ...Details: A sub-volume containing the filament was extracted from a tomogram, which was then 2D projected. The projected image was used for real space helical reconstruction to create the map. Resolution was estimated compared to molmap generation of PDB:3J0S at 20 angstroms in Chimera and correlation score of 0.93 was obtained. Number images used: 1 |
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Startup model | Type of model: NONE |
Final angle assignment | Type: NOT APPLICABLE |