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- EMDB-35302: Structure of mammalian spectrin-actin junctional complex of membr... -
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Basic information
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Title | Structure of mammalian spectrin-actin junctional complex of membrane skeleton, State II, Global map | |||||||||
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![]() | Macrocomplex / membrane skeleton / spectrin-actin junction / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() negative regulation of protein targeting to membrane / positive regulation of adherens junction organization / pointed-end actin filament capping / Gap junction degradation / Formation of annular gap junctions / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions ...negative regulation of protein targeting to membrane / positive regulation of adherens junction organization / pointed-end actin filament capping / Gap junction degradation / Formation of annular gap junctions / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / UCH proteinases / Clathrin-mediated endocytosis / Striated Muscle Contraction / spectrin / RHOF GTPase cycle / positive regulation of establishment of endothelial barrier / lens fiber cell development / myofibril assembly / spectrin-associated cytoskeleton / negative regulation of peptidyl-tyrosine phosphorylation / negative regulation of substrate adhesion-dependent cell spreading / platelet dense tubular network membrane / structural constituent of postsynaptic actin cytoskeleton / negative regulation of focal adhesion assembly / cell projection membrane / dense body / regulation of filopodium assembly / COP9 signalosome / actin filament capping / barbed-end actin filament capping / positive regulation of fibroblast migration / RHO GTPases activate IQGAPs / regulation of lamellipodium assembly / RHO GTPases Activate Formins / lamellipodium assembly / spectrin binding / cortical cytoskeleton / NuA4 histone acetyltransferase complex / tropomyosin binding / negative regulation of peptidyl-threonine phosphorylation / negative regulation of peptidyl-serine phosphorylation / striated muscle thin filament / actin filament bundle assembly / : / positive regulation of blood coagulation / erythrocyte development / cellular response to cAMP / cellular response to calcium ion / adult locomotory behavior / axonogenesis / cell projection / muscle contraction / cell motility / actin filament / regulation of actin cytoskeleton organization / actin filament organization / adherens junction / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / SH3 domain binding / : / actin filament binding / actin cytoskeleton / cell junction / actin binding / regulation of cell shape / cytoplasmic vesicle / actin cytoskeleton organization / protein-containing complex assembly / postsynaptic density / cytoskeleton / hydrolase activity / axon / focal adhesion / signaling receptor binding / synapse / protein kinase binding / perinuclear region of cytoplasm / protein-containing complex / ATP binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Li N / Chen S / Gao N | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of membrane skeleton organization in red blood cells. Authors: Ningning Li / Siyi Chen / Kui Xu / Meng-Ting He / Meng-Qiu Dong / Qiangfeng Cliff Zhang / Ning Gao / ![]() Abstract: The spectrin-based membrane skeleton is a ubiquitous membrane-associated two-dimensional cytoskeleton underneath the lipid membrane of metazoan cells. Mutations of skeleton proteins impair the ...The spectrin-based membrane skeleton is a ubiquitous membrane-associated two-dimensional cytoskeleton underneath the lipid membrane of metazoan cells. Mutations of skeleton proteins impair the mechanical strength and functions of the membrane, leading to several different types of human diseases. Here, we report the cryo-EM structures of the native spectrin-actin junctional complex (from porcine erythrocytes), which is a specialized short F-actin acting as the central organizational unit of the membrane skeleton. While an α-/β-adducin hetero-tetramer binds to the barbed end of F-actin as a flexible cap, tropomodulin and SH3BGRL2 together create an absolute cap at the pointed end. The junctional complex is strengthened by ring-like structures of dematin in the middle actin layers and by patterned periodic interactions with tropomyosin over its entire length. This work serves as a structural framework for understanding the assembly and dynamics of membrane skeleton and offers insights into mechanisms of various ubiquitous F-actin-binding factors in other F-actin systems. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.9 KB 24.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.9 KB | Display | ![]() |
Images | ![]() | 29.7 KB | ||
Filedesc metadata | ![]() | 8.7 KB | ||
Others | ![]() ![]() | 391.5 MB 391.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1002.5 KB | Display | ![]() |
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Full document | ![]() | 1002 KB | Display | |
Data in XML | ![]() | 24.6 KB | Display | |
Data in CIF | ![]() | 33 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8iaiMC ![]() 8iahC ![]() 8ib2C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Voxel size | X=Y=Z: 1.37 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_35302_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_35302_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Spectrin-actin junctional complex
+Supramolecule #1: Spectrin-actin junctional complex
+Macromolecule #1: Adducin 1
+Macromolecule #2: Beta-adducin
+Macromolecule #3: Dematin actin binding protein
+Macromolecule #4: Actin, cytoplasmic 1
+Macromolecule #5: Spectrin beta chain
+Macromolecule #6: Tropomyosin-1.9
+Macromolecule #7: Tropomyosin 3
+Macromolecule #8: Tropomodulin-1
+Macromolecule #9: SH3 domain-binding glutamic acid-rich-like protein
+Macromolecule #10: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 34.4 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 2.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |