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- EMDB-18302: Cryo-EM structure of Fts-Hook3-FHIP1B at 3.2 A resolution. -

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Basic information

Entry
Database: EMDB / ID: EMD-18302
TitleCryo-EM structure of Fts-Hook3-FHIP1B at 3.2 A resolution.
Map dataCryo-EM structure of FHF, comprising a C-terminal fragment of Hook3 (amino acids 571-718). B-factor applied: -116.705.
Sample
  • Complex: The Fts-Hook3-FHIP1B complex
    • Protein or peptide: Protein Hook homolog 3
    • Protein or peptide: FHF complex subunit HOOK-interacting protein 1B
    • Protein or peptide: AKT-interacting protein
Keywordsmotor proteins / molecular motors / cargo adaptors / bidirectional transport / microtubules / cytoskeleton. / PROTEIN TRANSPORT
Function / homology
Function and homology information


FHF complex / interkinetic nuclear migration / Golgi localization / protein localization to perinuclear region of cytoplasm / microtubule anchoring at centrosome / dynein light chain binding / cytoskeleton-dependent intracellular transport / neuronal stem cell population maintenance / endosome organization / NEDD8 transferase activity ...FHF complex / interkinetic nuclear migration / Golgi localization / protein localization to perinuclear region of cytoplasm / microtubule anchoring at centrosome / dynein light chain binding / cytoskeleton-dependent intracellular transport / neuronal stem cell population maintenance / endosome organization / NEDD8 transferase activity / early endosome to late endosome transport / cis-Golgi network / protein neddylation / dynein light intermediate chain binding / protein localization to centrosome / dynein intermediate chain binding / lysosome organization / endosome to lysosome transport / pericentriolar material / dynactin binding / cytoplasmic microtubule organization / centriolar satellite / negative regulation of neurogenesis / positive regulation of protein binding / protein transport / microtubule binding / microtubule / positive regulation of protein phosphorylation / apoptotic process / centrosome / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
FHF complex subunit HOOK interacting protein / FHF complex subunit HOOK interacting protein, KELAA motif / FHF complex subunit HOOK interacting protein, C-terminal / Retinoic acid induced 16-like protein / KELAA motif / Family of unknown function (DUF5917) / Hook, C-terminal / HOOK protein coiled-coil region / HOOK, N-terminal / HOOK domain ...FHF complex subunit HOOK interacting protein / FHF complex subunit HOOK interacting protein, KELAA motif / FHF complex subunit HOOK interacting protein, C-terminal / Retinoic acid induced 16-like protein / KELAA motif / Family of unknown function (DUF5917) / Hook, C-terminal / HOOK protein coiled-coil region / HOOK, N-terminal / HOOK domain / : / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like
Similarity search - Domain/homology
Protein Hook homolog 3 / FHF complex subunit HOOK-interacting protein 1B / AKT-interacting protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsAbid Ali F / Carter AP
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom) United Kingdom
Wellcome Trust United Kingdom
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: KIF1C activates and extends dynein movement through the FHF cargo adapter.
Authors: Ferdos Abid Ali / Alexander J Zwetsloot / Caroline E Stone / Tomos E Morgan / Richard F Wademan / Andrew P Carter / Anne Straube /
Abstract: Cellular cargos move bidirectionally on microtubules by recruiting opposite polarity motors dynein and kinesin. These motors show codependence, where one requires the activity of the other, although ...Cellular cargos move bidirectionally on microtubules by recruiting opposite polarity motors dynein and kinesin. These motors show codependence, where one requires the activity of the other, although the mechanism is unknown. Here we show that kinesin-3 KIF1C acts as both an activator and a processivity factor for dynein, using in vitro reconstitutions of human proteins. Activation requires only a fragment of the KIF1C nonmotor stalk binding the cargo adapter HOOK3. The interaction site is separate from the constitutive factors FTS and FHIP, which link HOOK3 to small G-proteins on cargos. We provide a structural model for the autoinhibited FTS-HOOK3-FHIP1B (an FHF complex) and explain how KIF1C relieves it. Collectively, we explain codependency by revealing how mutual activation of dynein and kinesin occurs through their shared adapter. Many adapters bind both dynein and kinesins, suggesting this mechanism could be generalized to other bidirectional complexes.
History
DepositionAug 23, 2023-
Header (metadata) releaseSep 4, 2024-
Map releaseSep 4, 2024-
UpdateApr 23, 2025-
Current statusApr 23, 2025Processing site: PDBe / Status: Released

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Structure visualization

Downloads & links

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Map

FileDownload / File: emd_18302.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM structure of FHF, comprising a C-terminal fragment of Hook3 (amino acids 571-718). B-factor applied: -116.705.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 256 pix.
= 271.104 Å		1.06 Å/pix.
x 256 pix.
= 271.104 Å		1.06 Å/pix.
x 256 pix.
= 271.104 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.059 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0185
Minimum - Maximum-0.06736556 - 0.12794802
Average (Standard dev.)0.000038062037 (±0.003249672)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 271.104 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_18302_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : The Fts-Hook3-FHIP1B complex

EntireName: The Fts-Hook3-FHIP1B complex
Components
  • Complex: The Fts-Hook3-FHIP1B complex
    • Protein or peptide: Protein Hook homolog 3
    • Protein or peptide: FHF complex subunit HOOK-interacting protein 1B
    • Protein or peptide: AKT-interacting protein

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Supramolecule #1: The Fts-Hook3-FHIP1B complex

SupramoleculeName: The Fts-Hook3-FHIP1B complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 305 KDa

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Macromolecule #1: Protein Hook homolog 3

MacromoleculeName: Protein Hook homolog 3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.394662 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
DLEPRFNNSS LKIEELQEAL RKKEEEMKQM EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE YEKTKSQRE MEEKYIVSAW YNMGMTLHKK AAEDRLASTG SGQSFLARQR QATSSRRSYP GHVQPATAR

UniProtKB: Protein Hook homolog 3

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Macromolecule #2: FHF complex subunit HOOK-interacting protein 1B

MacromoleculeName: FHF complex subunit HOOK-interacting protein 1B / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 105.64232 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MERMNWLSRL ASRGPGHRIP QGANLQTPVM ADPETCLMVF KNHWSQVVRI LERQGPRAAP GGADDLSAVR NHTYQMLTLL AEDRAVPSA PTGPGPLLEF ALHEDLLTRV LTWQLQWDEL GDGVEERRAE QLKLFEMLVS EARQPLLRHG PVREALLTLL D ACGRPVPS ...String:
MERMNWLSRL ASRGPGHRIP QGANLQTPVM ADPETCLMVF KNHWSQVVRI LERQGPRAAP GGADDLSAVR NHTYQMLTLL AEDRAVPSA PTGPGPLLEF ALHEDLLTRV LTWQLQWDEL GDGVEERRAE QLKLFEMLVS EARQPLLRHG PVREALLTLL D ACGRPVPS SPALDEGLVL LLSQLCVCVA QEPSLLEFFL QPPPEPGAAP RLLLFSRLVP FVHLEGTLGQ QARDALLLLM AL SAGSPTV GRYIADHSYF CPVLATGLSA LYSSLPRKIE VPGDDWHCLR REDWLGVPAL ALFMSSLEFC NAVIQVAHPL VQK QLVDYI HNGFLVPVMG PALHKTSVEE MIASTAYLEL FLRSISEPAL LRTFLRFLLL HRHDTHTILD TLVARIGSNS RLCM VSLSL FRTLLNLSCE DVLLQLVLRY LVPCNHVMLS QKPAVRDVDL YGRAADKFLS LIPRCCRHHA PSPPRPEHAS WARGP GSPS VDSSSVTTVP RPSTPSRLAL FLRQQSLGGS ESPGPAPCSP GLSASPASSP GRRPTPAEEP GELEDNYLEY LREARR GVD RCVRACRTWS APYDGERPSP EPSPFGSRTK KRSLLPEEDR NNVGEGEEEE LGRRGRAGGA GEGPGHLPPP QLNGVPG SW PEGAKKVRLV PKEGAGELLE GISEGMAGLE GFGQELRELE VALSNGGTGS ESPLEPPLPL EEEEAYESFT CPPEPPGP F LSSPLRTLNQ LPSQPFTGPF MAVLFAKLEN MLQNSVYVNF LLTGLVAQLA CHPQPLLRSF LLNTNMVFQP SVKSLLQVL GSVKNKIENF AASQEDFPAL LSKAKKYLIA RGKLDWAEGP AAGPAPRRSD PLVKSRRPSL GELLLRHAHS PTRARQAAQL VLQPGRDGA GLGLSGGSPG ASTPVLLTRG GAPERQGEAL RVKNAVYCAV IFPEFLKELA AISQAHAVTS PFLLETSEEG S GPLISGCG PLNP

UniProtKB: FHF complex subunit HOOK-interacting protein 1B

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Macromolecule #3: AKT-interacting protein

MacromoleculeName: AKT-interacting protein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 33.173977 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MNPFWSMSTS SVRKRSEGEE KTLTGDVKTS PPRTAPKKQL PSIPKNALPI TKPTSPAPAA QSTNGTHASY GPFYLEYSLL AEFTLVVKQ KLPGVYVQPS YRSALMWFGV IFIRHGLYQD GVFKFTVYIP DNYPDGDCPR LVFDIPVFHP LVDPTSGELD V KRAFAKWR ...String:
MNPFWSMSTS SVRKRSEGEE KTLTGDVKTS PPRTAPKKQL PSIPKNALPI TKPTSPAPAA QSTNGTHASY GPFYLEYSLL AEFTLVVKQ KLPGVYVQPS YRSALMWFGV IFIRHGLYQD GVFKFTVYIP DNYPDGDCPR LVFDIPVFHP LVDPTSGELD V KRAFAKWR RNHNHIWQVL MYARRVFYKI DTASPLNPEA AVLYEKDIQL FKSKVVDSVK VCTARLFDQP KIEDPYAISF SP WNPSVHD EAREKMLTQK KPEEQHNKSV HVAGLSWVKP GSVQPFSKEE KTVAT

UniProtKB: AKT-interacting protein

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 43.6 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 26.0 µm / Nominal defocus min: 16.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER / Details: de novo
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 273204
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model / Details: Initial model based on alphafold prediction of FHF
RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-8qat:
Cryo-EM structure of Fts-Hook3-FHIP1B at 3.2 A resolution.

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