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- PDB-8p94: Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleate... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8p94 | ||||||
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Title | Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches | ||||||
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![]() | CONTRACTILE PROTEIN / Complex | ||||||
Function / homology | ![]() cytoskeletal calyx / tubulobulbar complex / meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / meiotic cytokinesis / muscle cell projection membrane / lamellipodium organization / Advanced glycosylation endproduct receptor signaling / RHOF GTPase cycle ...cytoskeletal calyx / tubulobulbar complex / meiotic chromosome movement towards spindle pole / cytosolic transport / growth cone leading edge / meiotic cytokinesis / muscle cell projection membrane / lamellipodium organization / Advanced glycosylation endproduct receptor signaling / RHOF GTPase cycle / spindle localization / RHOD GTPase cycle / 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 / RHOF GTPase cycle / site of polarized growth / actin polymerization-dependent cell motility / COPI-independent Golgi-to-ER retrograde traffic / Arp2/3 protein complex / asymmetric cell division / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Arp2/3 complex-mediated actin nucleation / WASH complex / Arp2/3 complex binding / : / actin nucleation / F-actin capping protein complex / COPI-mediated anterograde transport / negative regulation of filopodium assembly / modification of postsynaptic actin cytoskeleton / modification of postsynaptic structure / mitotic spindle midzone / regulation of cell projection assembly / actin cap / regulation of mitophagy / postsynaptic actin cytoskeleton / structural constituent of postsynaptic actin cytoskeleton / profilin binding / Factors involved in megakaryocyte development and platelet production / dense body / positive regulation of smooth muscle contraction / regulation of actin filament polymerization / positive regulation of chemotaxis / substrate-dependent cell migration, cell extension / cell projection organization / MHC class II antigen presentation / cell junction assembly / barbed-end actin filament capping / actin polymerization or depolymerization / focal adhesion assembly / regulation of cell morphogenesis / podosome / proline-rich region binding / regulation of lamellipodium assembly / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / dendritic spine maintenance / lamellipodium assembly / regulation of axon extension / establishment or maintenance of cell polarity / cortical actin cytoskeleton / cortical cytoskeleton / positive regulation of actin filament polymerization / NuA4 histone acetyltransferase complex / filamentous actin / brush border / positive regulation of double-strand break repair via homologous recombination / asymmetric synapse / cilium assembly / RHO GTPases Activate WASPs and WAVEs / positive regulation of lamellipodium assembly / extrinsic apoptotic signaling pathway / positive regulation of substrate adhesion-dependent cell spreading / clathrin-coated pit / voltage-gated potassium channel complex / ruffle / cytoskeleton organization / EPHB-mediated forward signaling / actin filament polymerization / hippocampal mossy fiber to CA3 synapse / axonogenesis / neuron projection morphogenesis / receptor-mediated endocytosis / cellular response to nerve growth factor stimulus / cell projection / cell motility / actin filament / negative regulation of extrinsic apoptotic signaling pathway / FCGR3A-mediated phagocytosis / intracellular protein transport / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||
![]() | Liu, T. / Moores, C.A. | ||||||
Funding support | European Union, 1items
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![]() | ![]() Title: Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament. Authors: Tianyang Liu / Luyan Cao / Miroslav Mladenov / Antoine Jegou / Michael Way / Carolyn A Moores / ![]() ![]() Abstract: Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane ...Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane trafficking. Cortactin is important for actin branch stabilization, but the mechanism by which this occurs is unclear. Given this, we determined the structure of vertebrate cortactin-stabilized Arp2/3 actin branches using cryogenic electron microscopy. We find that cortactin interacts with the new daughter filament nucleated by the Arp2/3 complex at the branch site, rather than the initial mother actin filament. Cortactin preferentially binds activated Arp3. It also stabilizes the F-actin-like interface of activated Arp3 with the first actin subunit of the new filament, and its central repeats extend along successive daughter-filament subunits. The preference of cortactin for activated Arp3 explains its retention at the actin branch and accounts for its synergy with other nucleation-promoting factors in regulating branched actin network dynamics. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.1 MB | Display | ![]() |
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Full document | ![]() | 2.1 MB | Display | |
Data in XML | ![]() | 161 KB | Display | |
Data in CIF | ![]() | 252.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 17558MC C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Actin-related protein ... , 7 types, 7 molecules ABCDEFG
#1: Protein | Mass: 47428.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 44818.711 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Protein | Mass: 41004.781 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#4: Protein | Mass: 34386.043 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#5: Protein | Mass: 20572.666 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#6: Protein | Mass: 19697.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#7: Protein | Mass: 16964.180 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein , 4 types, 13 molecules HJKNOPQRSWIUV
#8: Protein | Mass: 41782.660 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #9: Protein | | Mass: 61340.738 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #10: Protein | | Mass: 32980.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #11: Protein | | Mass: 30669.768 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Protein/peptide , 1 types, 10 molecules abcdhijklm
#12: Protein/peptide | Type: Peptide-like / Class: Toxin / Mass: 808.899 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 2 types, 24 molecules ![](data/chem/img/ADP.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/MG.gif)
#13: Chemical | ChemComp-ADP / #14: Chemical | ChemComp-MG / |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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Source (recombinant) |
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Buffer solution | pH: 7.5 Details: 20 mM HEPES pH 7.5, 50mM KCl, 1mM EGTA, 1mM MgCl2, 0.2 mM ATP and 1 mM DTT | ||||||||||||||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||||||||
Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 98 % / Chamber temperature: 295.15 K / Details: Back blotting |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2400 nm / Nominal defocus min: 900 nm |
Image recording | Electron dose: 49.4 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
EM software |
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CTF correction | Details: CryoSPARC Patch CTF / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 2001580 | ||||||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 130915 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||
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Atomic model building |
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