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- PDB-8yao: Cryo-ET structure of huntingtin actin dimer complex -

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Basic information

Entry
Database: PDB / ID: 8yao
TitleCryo-ET structure of huntingtin actin dimer complex
Components
  • Actin, alpha skeletal muscle
  • Huntingtin
KeywordsCYTOSOLIC PROTEIN/CONTRACTILE PROTEIN / Huntington's disease / cytoskeleton / CYTOSOLIC PROTEIN / CYTOSOLIC PROTEIN-CONTRACTILE PROTEIN complex
Function / homology
Function and homology information


: / positive regulation of CAMKK-AMPK signaling cascade / microtubule-based transport / vocal learning / positive regulation of mitophagy / regulation of CAMKK-AMPK signaling cascade / profilin binding / positive regulation of cilium assembly / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / vesicle transport along microtubule ...: / positive regulation of CAMKK-AMPK signaling cascade / microtubule-based transport / vocal learning / positive regulation of mitophagy / regulation of CAMKK-AMPK signaling cascade / profilin binding / positive regulation of cilium assembly / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / vesicle transport along microtubule / positive regulation of aggrephagy / positive regulation of lipophagy / cytoskeletal motor activator activity / myosin heavy chain binding / tropomyosin binding / actin filament bundle / Golgi organization / troponin I binding / filamentous actin / mesenchyme migration / dynein intermediate chain binding / establishment of mitotic spindle orientation / actin filament bundle assembly / phosphoprotein phosphatase activity / dynactin binding / skeletal muscle myofibril / striated muscle thin filament / skeletal muscle thin filament assembly / Regulation of MECP2 expression and activity / actin monomer binding / postsynaptic cytosol / beta-tubulin binding / presynaptic cytosol / skeletal muscle fiber development / stress fiber / titin binding / heat shock protein binding / inclusion body / actin filament polymerization / centriole / autophagosome / cytoplasmic vesicle membrane / negative regulation of extrinsic apoptotic signaling pathway / actin filament / filopodium / protein destabilization / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / kinase binding / calcium-dependent protein binding / p53 binding / late endosome / lamellipodium / cell body / transmembrane transporter binding / early endosome / hydrolase activity / positive regulation of apoptotic process / protein domain specific binding / axon / apoptotic process / calcium ion binding / dendrite / positive regulation of gene expression / perinuclear region of cytoplasm / magnesium ion binding / endoplasmic reticulum / Golgi apparatus / protein-containing complex / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Huntingtin / Huntingtin, middle-repeat / Huntingtin family / : / : / : / Huntingtin, N-terminal HEAT / Huntingtin, bridge / Huntingtin, N-terminal HEAT 1 / Huntingtin, C-terminal HEAT ...Huntingtin / Huntingtin, middle-repeat / Huntingtin family / : / : / : / Huntingtin, N-terminal HEAT / Huntingtin, bridge / Huntingtin, N-terminal HEAT 1 / Huntingtin, C-terminal HEAT / 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 / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
Huntingtin / Actin, alpha skeletal muscle
Similarity search - Component
Biological speciesHomo sapiens (human)
Oryctolagus cuniculus (rabbit)
MethodELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 20.8 Å
AuthorsKim, J. / Kim, H. / Fassler, F. / Hansen, J.M. / Schur, F.K.M. / Song, J.J.
Funding support Korea, Republic Of, 1items
OrganizationGrant numberCountry
National Research Foundation (NRF, Korea) Korea, Republic Of
CitationJournal: Sci Adv / Year: 2025
Title: Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization.
Authors: Rémi Carpentier / Jaesung Kim / Mariacristina Capizzi / Hyeongju Kim / Florian Fäßler / Jesse M Hansen / Min Jeong Kim / Eric Denarier / Béatrice Blot / Marine Degennaro / Sophia Labou / ...Authors: Rémi Carpentier / Jaesung Kim / Mariacristina Capizzi / Hyeongju Kim / Florian Fäßler / Jesse M Hansen / Min Jeong Kim / Eric Denarier / Béatrice Blot / Marine Degennaro / Sophia Labou / Isabelle Arnal / Maria J Marcaida / Matteo Dal Peraro / Doory Kim / Florian K M Schur / Ji-Joon Song / Sandrine Humbert /
Abstract: The Huntingtin protein (HTT), named for its role in Huntington's disease, has been best understood as a scaffolding protein that promotes vesicle transport by molecular motors along microtubules. ...The Huntingtin protein (HTT), named for its role in Huntington's disease, has been best understood as a scaffolding protein that promotes vesicle transport by molecular motors along microtubules. Here, we show that HTT also interacts with the actin cytoskeleton, and its loss of function disturbs the morphology and function of the axonal growth cone. We demonstrate that HTT organizes F-actin into bundles. Cryo-electron tomography (cryo-ET) and subtomogram averaging (STA) structural analyses reveal that HTT's N-terminal HEAT and Bridge domains wrap around F-actin, while the C-terminal HEAT domain is displaced; furthermore, HTT dimerizes via the N-HEAT domain to bridge parallel actin filaments separated by ~20 nanometers. Our study provides the structural basis for understanding how HTT interacts with and organizes the actin cytoskeleton.
History
DepositionFeb 9, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Aug 13, 2025Provider: repository / Type: Initial release
Revision 1.0Aug 13, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
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Revision 1.1Aug 27, 2025Group: Data collection / Database references / Structure summary
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Huntingtin
N: Actin, alpha skeletal muscle
B: Actin, alpha skeletal muscle
C: Actin, alpha skeletal muscle
D: Actin, alpha skeletal muscle
E: Actin, alpha skeletal muscle
F: Actin, alpha skeletal muscle
G: Actin, alpha skeletal muscle
H: Actin, alpha skeletal muscle
I: Actin, alpha skeletal muscle
J: Actin, alpha skeletal muscle
K: Actin, alpha skeletal muscle
L: Actin, alpha skeletal muscle
M: Actin, alpha skeletal muscle
a: Huntingtin
n: Actin, alpha skeletal muscle
b: Actin, alpha skeletal muscle
c: Actin, alpha skeletal muscle
d: Actin, alpha skeletal muscle
e: Actin, alpha skeletal muscle
f: Actin, alpha skeletal muscle
g: Actin, alpha skeletal muscle
h: Actin, alpha skeletal muscle
i: Actin, alpha skeletal muscle
j: Actin, alpha skeletal muscle
k: Actin, alpha skeletal muscle
l: Actin, alpha skeletal muscle
m: Actin, alpha skeletal muscle


Theoretical massNumber of molelcules
Total (without water)1,784,68428
Polymers1,784,68428
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Huntingtin / Huntington disease protein / HD protein


Mass: 348128.094 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HTT, HD, IT15 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P42858
#2: Protein ...
Actin, alpha skeletal muscle / Alpha-actin-1


Mass: 41862.613 Da / Num. of mol.: 26 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / References: UniProt: P68135
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: subtomogram averaging

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Sample preparation

ComponentName: Huntingtin-Actin complex / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 6000 nm / Nominal defocus min: 2000 nm
Image recordingElectron dose: 170 e/Å2 / Avg electron dose per subtomogram: 2.79 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 20.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 21000 / Symmetry type: POINT
EM volume selectionNum. of tomograms: 42 / Num. of volumes extracted: 84019
Atomic model buildingProtocol: RIGID BODY FIT

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