|Entry||Database: PDB / ID: 7pdz|
|Title||Structure of capping protein bound to the barbed end of a cytoplasmic actin filament|
|Keywords||STRUCTURAL PROTEIN / Cytoskeleton / cell-shape remodelling / barbed end|
|Function / homology|
Function and homology information
cytoskeletal calyx / regulation of protein kinase C signaling / Advanced glycosylation endproduct receptor signaling / COPI-independent Golgi-to-ER retrograde traffic / WASH complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / sperm head / negative regulation of filopodium assembly / COPI-mediated anterograde transport / sperm connecting piece ...cytoskeletal calyx / regulation of protein kinase C signaling / Advanced glycosylation endproduct receptor signaling / COPI-independent Golgi-to-ER retrograde traffic / WASH complex / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / sperm head / negative regulation of filopodium assembly / COPI-mediated anterograde transport / sperm connecting piece / F-actin capping protein complex / muscle cell development => GO:0055001 / structural constituent of postsynaptic actin cytoskeleton / dense body / cell projection organization / Factors involved in megakaryocyte development and platelet production / MHC class II antigen presentation / barbed-end actin filament capping / actin polymerization or depolymerization / NuA4 histone acetyltransferase complex / regulation of cell morphogenesis / negative regulation of microtubule polymerization / regulation of lamellipodium assembly / cell junction assembly / beta-tubulin binding / lamellipodium assembly / cortical cytoskeleton / brush border / asymmetric synapse / synaptic vesicle endocytosis / intercalated disc / calyx of Held / cell motility / cytoskeleton organization / axonogenesis / hippocampal mossy fiber to CA3 synapse / Schaffer collateral - CA1 synapse / actin filament / cell morphogenesis / actin cytoskeleton organization / Z disc / negative regulation of protein binding / neuron projection development / actin cytoskeleton / cell-cell junction / lamellipodium / actin binding / dendritic spine / postsynaptic density / cytoskeleton / synapse / axon / focal adhesion / neuronal cell body / protein kinase binding / protein-containing complex / membrane / ATP binding / plasma membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
F-actin capping protein, beta subunit / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit, conserved site / F-actin capping protein beta subunit signature. / F-actin-capping protein subunit beta / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 2. / F-actin capping protein alpha subunit signature 1. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta, domain 2 ...F-actin capping protein, beta subunit / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit, conserved site / F-actin capping protein beta subunit signature. / F-actin-capping protein subunit beta / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 2. / F-actin capping protein alpha subunit signature 1. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin-capping protein subunit alpha/beta / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / Actins signature 1. / Actins signature 2. / Actin, conserved site / Actins and actin-related proteins signature. / Actin/actin-like conserved site / Actin / Actin family / Actin / ATPase, nucleotide binding domain
Similarity search - Domain/homology
F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Phalloidin / ADENOSINE-5'-DIPHOSPHATE / PHOSPHATE ION / Actin, cytoplasmic 1
Similarity search - Component
|Biological species||Mus musculus (house mouse)|
Bos taurus (cattle)
synthetic construct (others)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å|
|Authors||Funk, J. / Merino, F. / Schacks, M. / Rottner, K. / Raunser, S. / Bieling, P.|
|Funding support|| Germany, 1items |
|Citation||Journal: Nat Commun / Year: 2021|
Title: A barbed end interference mechanism reveals how capping protein promotes nucleation in branched actin networks.
Authors: Johanna Funk / Felipe Merino / Matthias Schaks / Klemens Rottner / Stefan Raunser / Peter Bieling /
Abstract: Heterodimeric capping protein (CP/CapZ) is an essential factor for the assembly of branched actin networks, which push against cellular membranes to drive a large variety of cellular processes. Aside ...Heterodimeric capping protein (CP/CapZ) is an essential factor for the assembly of branched actin networks, which push against cellular membranes to drive a large variety of cellular processes. Aside from terminating filament growth, CP potentiates the nucleation of actin filaments by the Arp2/3 complex in branched actin networks through an unclear mechanism. Here, we combine structural biology with in vitro reconstitution to demonstrate that CP not only terminates filament elongation, but indirectly stimulates the activity of Arp2/3 activating nucleation promoting factors (NPFs) by preventing their association to filament barbed ends. Key to this function is one of CP's C-terminal "tentacle" extensions, which sterically masks the main interaction site of the terminal actin protomer. Deletion of the β tentacle only modestly impairs capping. However, in the context of a growing branched actin network, its removal potently inhibits nucleation promoting factors by tethering them to capped filament ends. End tethering of NPFs prevents their loading with actin monomers required for activation of the Arp2/3 complex and thus strongly inhibits branched network assembly both in cells and reconstituted motility assays. Our results mechanistically explain how CP couples two opposed processes-capping and nucleation-in branched actin network assembly.
|Structure viewer||Molecule: |
Downloads & links
E: Isoform 2 of F-actin-capping protein subunit beta
F: F-actin-capping protein subunit alpha-1
I: Actin, cytoplasmic 1
J: Actin, cytoplasmic 1
K: Actin, cytoplasmic 1
L: Actin, cytoplasmic 1
N: Actin, cytoplasmic 1
O: Actin, cytoplasmic 1
-Protein , 3 types, 8 molecules E
F I J K L N O
|#1: Protein|| |
Mass: 30669.768 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Capzb, Cappb1 / Production host: Escherichia coli (E. coli) / References: UniProt: P47757
|#2: Protein|| |
Mass: 32980.703 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Capza1, Cappa1 / Production host: Escherichia coli (E. coli) / References: UniProt: P47753
Mass: 41795.680 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P60712
-Protein/peptide , 1 types, 5 molecules Q
R S T P
-Non-polymers , 3 types, 16 molecules
Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
|Has ligand of interest||Y|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Complex between capping protein and the barbed end of cytoplasmic actin filaments|
Type: COMPLEX / Entity ID: #1-#4 / Source: MULTIPLE SOURCES
|Molecular weight||Experimental value: NO|
|Buffer solution||pH: 7 / Details: KMEI buffer|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Details: Mild discharging with 5 mA current / Grid material: COPPER / Grid type: Quantifoil R1.2/1.3|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 286 K|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Microscopy||Model: FEI TALOS ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Alignment procedure: COMA FREE|
|Specimen holder||Cryogen: NITROGEN|
|Image recording||Average exposure time: 3 sec. / Electron dose: 60 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 4204|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Particle selection||Num. of particles selected: 570724|
|3D reconstruction||Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 60206 / Algorithm: BACK PROJECTION / Num. of class averages: 1 / Symmetry type: POINT|
|Atomic model building||B value: 40 / Protocol: FLEXIBLE FIT / Space: REAL|
|Atomic model building||PDB-ID: 5ADX|
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