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Entry
Database: EMDB / ID: EMD-53107
TitleCryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands
Map dataMain, sharpened cryo-EM density map of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands
Sample
  • Complex: Beta-actin filament hetero-decorated by Coronin-1B and Cofilin-1.
    • Complex: Actin filament
      • Protein or peptide: Actin, cytoplasmic 1, N-terminally processed
    • Complex: Coronin-1B
      • Protein or peptide: Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase
    • Complex: Cofilin-1
      • Protein or peptide: Cofilin-1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
Keywordsactin / coronin / cofilin / filament / cytoskeleton / STRUCTURAL PROTEIN
Function / homology
Function and homology information


actin filament branching / MGMT-mediated DNA damage reversal / cellular response to ether / cofilin-actin rod / positive regulation of protein localization to cell leading edge / positive regulation of establishment of cell polarity regulating cell shape / negative regulation of unidimensional cell growth / positive regulation of barbed-end actin filament capping / neural fold formation / negative regulation of lamellipodium assembly ...actin filament branching / MGMT-mediated DNA damage reversal / cellular response to ether / cofilin-actin rod / positive regulation of protein localization to cell leading edge / positive regulation of establishment of cell polarity regulating cell shape / negative regulation of unidimensional cell growth / positive regulation of barbed-end actin filament capping / neural fold formation / negative regulation of lamellipodium assembly / negative regulation of postsynaptic density organization / protein localization to cell leading edge / actin filament fragmentation / methylated-DNA-[protein]-cysteine S-methyltransferase / methylated-DNA-[protein]-cysteine S-methyltransferase activity / Arp2/3 complex binding / positive regulation of actin filament depolymerization / negative regulation of smooth muscle cell chemotaxis / modification of postsynaptic actin cytoskeleton / regulation of Arp2/3 complex-mediated actin nucleation / positive regulation of embryonic development / positive regulation of norepinephrine uptake / DNA-methyltransferase activity / negative regulation of actin filament bundle assembly / negative regulation of Arp2/3 complex-mediated actin nucleation / positive regulation of synaptic plasticity / endothelial cell chemotaxis / negative regulation of actin filament depolymerization / cellular response to cytochalasin B / bBAF complex / npBAF complex / actin filament severing / nBAF complex / brahma complex / regulation of transepithelial transport / Formation of annular gap junctions / morphogenesis of a polarized epithelium / Formation of the dystrophin-glycoprotein complex (DGC) / structural constituent of postsynaptic actin cytoskeleton / Gap junction degradation / GBAF complex / Folding of actin by CCT/TriC / protein localization to adherens junction / establishment of spindle localization / regulation of G0 to G1 transition / regulation of dendritic spine morphogenesis / Cell-extracellular matrix interactions / host-mediated activation of viral process / actin filament depolymerization / dense body / Tat protein binding / cell projection organization / ruffle organization / postsynaptic actin cytoskeleton / negative regulation of cell adhesion / DNA alkylation repair / negative regulation of cell motility / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / RHO GTPases Activate ROCKs / negative regulation of cell size / regulation of double-strand break repair / regulation of nucleotide-excision repair / cellular response to interleukin-6 / regulation of cell morphogenesis / Adherens junctions interactions / RHOF GTPase cycle / negative regulation of dendritic spine maintenance / adherens junction assembly / positive regulation of lamellipodium morphogenesis / apical protein localization / Sensory processing of sound by outer hair cells of the cochlea / neural crest cell migration / Interaction between L1 and Ankyrins / tight junction / regulation of mitotic metaphase/anaphase transition / SWI/SNF complex / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of cell motility / positive regulation of T cell differentiation / cortical actin cytoskeleton / apical junction complex / phosphatidylinositol bisphosphate binding / cellular response to insulin-like growth factor stimulus / positive regulation of double-strand break repair / maintenance of blood-brain barrier / regulation of norepinephrine uptake / nitric-oxide synthase binding / transporter regulator activity / establishment of cell polarity / positive regulation of dendritic spine development / cortical cytoskeleton / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / positive regulation of stem cell population maintenance / cell leading edge / Recycling pathway of L1 / Regulation of MITF-M-dependent genes involved in pigmentation / brush border / mitotic cytokinesis
Similarity search - Function
Domain of unknown function DUF1899 / Coronin / Domain of unknown function (DUF1899) / Type of WD40 repeat / DUF1899 / DUF1900 / ADF/Cofilin / Methylguanine DNA methyltransferase, ribonuclease-like domain / 6-O-methylguanine DNA methyltransferase, ribonuclease-like domain / Methylated DNA-protein cysteine methyltransferase domain superfamily ...Domain of unknown function DUF1899 / Coronin / Domain of unknown function (DUF1899) / Type of WD40 repeat / DUF1899 / DUF1900 / ADF/Cofilin / Methylguanine DNA methyltransferase, ribonuclease-like domain / 6-O-methylguanine DNA methyltransferase, ribonuclease-like domain / Methylated DNA-protein cysteine methyltransferase domain superfamily / Methylated-DNA-[protein]-cysteine S-methyltransferase, active site / Methylated-DNA--protein-cysteine methyltransferase active site. / Methylated-DNA-[protein]-cysteine S-methyltransferase, DNA binding / Methylated DNA-protein cysteine methyltransferase, DNA binding domain / 6-O-methylguanine DNA methyltransferase, DNA binding domain / Actin-depolymerising factor homology domain / Cofilin/tropomyosin-type actin-binding protein / ADF-H domain profile. / Actin depolymerisation factor/cofilin -like domains / ADF-H/Gelsolin-like domain superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / WD domain, G-beta repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / Winged helix-like DNA-binding domain superfamily / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Methylated-DNA--protein-cysteine methyltransferase / Cofilin-1 / Actin, cytoplasmic 1 / Coronin-1B
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.12 Å
AuthorsOosterheert W / Boiero Sanders M / Hofnagel O / Bieling P / Raunser S
Funding support Germany, European Union, 4 items
OrganizationGrant numberCountry
Max Planck Society Germany
Alexander von Humboldt Foundation Germany
German Research Foundation (DFG)BI 1998/2-1 Germany
European Research Council (ERC)856118European Union
CitationJournal: Cell / Year: 2025
Title: Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1.
Authors: Wout Oosterheert / Micaela Boiero Sanders / Oliver Hofnagel / Peter Bieling / Stefan Raunser /
Abstract: Rapid remodeling of actin filament (F-actin) networks is essential for the movement and morphogenesis of eukaryotic cells. The conserved actin-binding proteins coronin, cofilin, and actin-interacting ...Rapid remodeling of actin filament (F-actin) networks is essential for the movement and morphogenesis of eukaryotic cells. The conserved actin-binding proteins coronin, cofilin, and actin-interacting protein 1 (AIP1) act in synergy to promote rapid F-actin network disassembly, but the underlying mechanisms have remained elusive. Here, using cryo-electron microscopy (cryo-EM), we uncover the concerted molecular actions of coronin, cofilin, and AIP1 that lead to actin filament aging and severing. We find that the cooperative binding of coronin allosterically promotes inorganic phosphate release from F-actin and induces filament undertwisting, thereby priming the filament for cofilin binding. Cofilin then displaces coronin from the filament via a strand-restricted cooperative binding mechanism. The resulting cofilactin serves as a high-affinity platform for AIP1, which induces severing by acting as a clamp that disrupts inter-subunit filament contacts. In this "molecular squeezing" mechanism, AIP1 and not cofilin is responsible for filament severing. Our work redefines the role of key disassembly factors in actin dynamics.
History
DepositionMar 11, 2025-
Header (metadata) releaseOct 8, 2025-
Map releaseOct 8, 2025-
UpdateOct 22, 2025-
Current statusOct 22, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_53107.png

Downloads & links

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Map

FileDownload / File: emd_53107.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMain, sharpened cryo-EM density map of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.68 Å/pix.
x 600 pix.
= 408. Å		0.68 Å/pix.
x 600 pix.
= 408. Å		0.68 Å/pix.
x 600 pix.
= 408. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.68 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0329
Minimum - Maximum-0.10507203 - 0.18655688
Average (Standard dev.)0.00010262156 (±0.005965612)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions600600600
Spacing600600600
CellA=B=C: 408.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_53107_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Additional unsharpened map of the actin filament hetero-decorated...

Fileemd_53107_additional_1.map
AnnotationAdditional unsharpened map of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A of the actin filament hetero-decorated...

Fileemd_53107_half_map_1.map
AnnotationHalf map A of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B of the actin filament hetero-decorated...

Fileemd_53107_half_map_2.map
AnnotationHalf map B of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Beta-actin filament hetero-decorated by Coronin-1B and Cofilin-1.

EntireName: Beta-actin filament hetero-decorated by Coronin-1B and Cofilin-1.
Components
  • Complex: Beta-actin filament hetero-decorated by Coronin-1B and Cofilin-1.
    • Complex: Actin filament
      • Protein or peptide: Actin, cytoplasmic 1, N-terminally processed
    • Complex: Coronin-1B
      • Protein or peptide: Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase
    • Complex: Cofilin-1
      • Protein or peptide: Cofilin-1
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Beta-actin filament hetero-decorated by Coronin-1B and Cofilin-1.

SupramoleculeName: Beta-actin filament hetero-decorated by Coronin-1B and Cofilin-1.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Actin filament

SupramoleculeName: Actin filament / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Details: Assembled as a double stranded helix of beta-actin subunits.
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Coronin-1B

SupramoleculeName: Coronin-1B / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #3
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Cofilin-1

SupramoleculeName: Cofilin-1 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Actin, cytoplasmic 1, N-terminally processed

MacromoleculeName: Actin, cytoplasmic 1, N-terminally processed / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.632422 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: DDDIAALVVD NGSGMCKAGF AGDDAPRAVF PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI E(HIC)GIVT NWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGD GV THTVPIYEGY ...String:
DDDIAALVVD NGSGMCKAGF AGDDAPRAVF PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI E(HIC)GIVT NWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGD GV THTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLE K SYELPDGQVI TIGNERFRCP EALFQPSFLG MESAGIHETT FNSIMKCDVD IRKDLYANTV LSGGTTMYPG IADRMQKEI TALAPSTMKI KIIAPPERKY SVWIGGSILA SLSTFQQMWI SKQEYDESGP SIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #2: Cofilin-1

MacromoleculeName: Cofilin-1 / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.532531 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATY ETKESKKEDL VFIFWAPESA PLKSKMIYAS SKDAIKKKLT GIKHELQANC YEEVKDRCTL AEKLGGSAVI S LEGKPL

UniProtKB: Cofilin-1

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Macromolecule #3: Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase

MacromoleculeName: Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase
type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
EC number: methylated-DNA-[protein]-cysteine S-methyltransferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 74.788086 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GAMGSMSFRK VVRQSKFRHV FGQPVKNDQC YEDIRVSRVT WDSTFCAVNP KFLAVIVEAS GGGAFLVLPL SKTGRIDKAY PTVCGHTGP VLDIDWCPHN DEVIASGSED CTVMVWQIPE NGLTSPLTEP VVVLEGHTKR VGIIAWHPTA RNVLLSAGCD N VVLIWNVG ...String:
GAMGSMSFRK VVRQSKFRHV FGQPVKNDQC YEDIRVSRVT WDSTFCAVNP KFLAVIVEAS GGGAFLVLPL SKTGRIDKAY PTVCGHTGP VLDIDWCPHN DEVIASGSED CTVMVWQIPE NGLTSPLTEP VVVLEGHTKR VGIIAWHPTA RNVLLSAGCD N VVLIWNVG TAEELYRLDS LHPDLIYNVS WNHNGSLFCS ACKDKSVRII DPRRGTLVAE REKAHEGARP MRAIFLADGK VF TTGFSRM SERQLALWDP ENLEEPMALQ ELDSSNGALL PFYDPDTSVV YVCGKGDSSI RYFEITEEPP YIHFLNTFTS KEP QRGMGS MPKRGLEVSK CEIARFYKLH ERKCEPIVMT VPRKSDLFQD DLYPDTAGPE AALEAEEWVS GRDADPILIS LREA YVPSK QRDLKISRRN VLSDSRPAMA PGSSHLGAPA STTTAADATP SGSLARAGEA GKLEEVMQEL RALRALVKEQ GDRIC RLEE QLGRMENGDA GTGGGGSGGG GSMDKDCEMK RTTLDSPLGK LELSGCEQGL HEIKLLGKGT SAADAVEVPA PAAVLG GPE PLMQATAWLN AYFHQPEAIE EFPVPALHHP VFQQESFTRQ VLWKLLKVVK FGEVISYQQL AALAGNPAAT AAVKTAL SG NPVPILIPCH RVVSSSGAVG GYEGGLAVKE WLLAHEGHRL GKPGLG

UniProtKB: Coronin-1B, Methylated-DNA--protein-cysteine methyltransferase

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Macromolecule #4: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 7 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #5: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 5 / Number of copies: 7 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statefilament

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Sample preparation

BufferpH: 7.1
Component:
ConcentrationNameFormula
10.0 mMHEPES
100.0 mMpotassium chlorideKCl
2.0 mMmagnesium chlorideMgCl2
1.0 mMEGTA
0.5 mMTCEP
0.02 % (v/v)Tween20

Details: 1xKMEH (10 mM HEPES pH 7.1, 100 mM KCl, 2 mM MgCl2, 1 mM EGTA, 0.5 mM TCEP, 0.02% Tween20).
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 90 sec.
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 286 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsSpherical aberration corrector: The used Titan Krios G2 microscope contains an in-column Cs corrector.
Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 15 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 14055 / Average electron dose: 65.8 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 2.7 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 10071093
CTF correctionSoftware - Name: cryoSPARC (ver. 4.4) / Software - details: Patch CTF / Details: Patch CTF / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
EMDB ID:

53096

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.12 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.4) / Software - details: Helical Refinement / Number images used: 40453
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.4) / Details: CryoSPARC
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.4)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 4.4)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

9qf2


Chain - Source name: PDB / Chain - Initial model type: experimental model
DetailsPhenix real space refinement.
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9qfe:
Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands

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