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- EMDB-48504: Cryo-EM structure of VCP bound to p47 UBX domain and VCPIP1 VCPID... -

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Basic information

Entry
Database: EMDB / ID: EMD-48504
TitleCryo-EM structure of VCP bound to p47 UBX domain and VCPIP1 VCPIDs (with stalk region)
Map data
Sample
  • Complex: Complex of valosin containing protein (VCP)/p97 bound to valosin containing protein interacting protein 1 (VCPIP1) and p47
    • Complex: Valosin containing protein (VCP)
      • Protein or peptide: Transitional endoplasmic reticulum ATPase
    • Complex: Valosin containing protein interacting protein 1 (VCPIP1)
      • Protein or peptide: Deubiquitinating protein VCPIP1
    • Complex: p47
      • Protein or peptide: NSFL1 cofactor p47
Keywordsdouble-ring hexameric complex / valosin containing protein / ATPase / VCP / mammalian / DUB / deubiquitinase / deubiquitinating enzyme / VCIP135 / p97 / VCPIP1 / hydrolase / VCPID / p47 / adapter / SHP / UBX / TRANSLOCASE
Function / homology
Function and homology information


negative regulation of protein localization to centrosome / positive regulation of mitotic centrosome separation / protein K11-linked deubiquitination / endoplasmic reticulum membrane fusion / Golgi reassembly / nuclear membrane reassembly / protein K48-linked deubiquitination / : / flavin adenine dinucleotide catabolic process / VCP-NSFL1C complex ...negative regulation of protein localization to centrosome / positive regulation of mitotic centrosome separation / protein K11-linked deubiquitination / endoplasmic reticulum membrane fusion / Golgi reassembly / nuclear membrane reassembly / protein K48-linked deubiquitination / : / flavin adenine dinucleotide catabolic process / VCP-NSFL1C complex / endosome to lysosome transport via multivesicular body sorting pathway / endoplasmic reticulum stress-induced pre-emptive quality control / BAT3 complex binding / cellular response to arsenite ion / protein-DNA covalent cross-linking repair / Derlin-1 retrotranslocation complex / positive regulation of protein K63-linked deubiquitination / cytoplasm protein quality control / positive regulation of oxidative phosphorylation / : / Golgi stack / aggresome assembly / deubiquitinase activator activity / ubiquitin-modified protein reader activity / mitotic spindle disassembly / regulation of protein localization to chromatin / VCP-NPL4-UFD1 AAA ATPase complex / cellular response to misfolded protein / negative regulation of protein localization to chromatin / positive regulation of mitochondrial membrane potential / vesicle-fusing ATPase / K48-linked polyubiquitin modification-dependent protein binding / regulation of aerobic respiration / retrograde protein transport, ER to cytosol / stress granule disassembly / ATPase complex / regulation of synapse organization / ubiquitin-specific protease binding / Golgi organization / MHC class I protein binding / positive regulation of ATP biosynthetic process / ubiquitin-like protein ligase binding / establishment of mitotic spindle orientation / RHOH GTPase cycle / polyubiquitin modification-dependent protein binding / autophagosome assembly / protein deubiquitination / autophagosome maturation / negative regulation of hippo signaling / endoplasmic reticulum to Golgi vesicle-mediated transport / HSF1 activation / translesion synthesis / interstrand cross-link repair / ATP metabolic process / proteasomal protein catabolic process / endoplasmic reticulum unfolded protein response / Protein methylation / Attachment and Entry / ERAD pathway / lipid droplet / proteasome complex / viral genome replication / Josephin domain DUBs / ubiquitin binding / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / negative regulation of smoothened signaling pathway / macroautophagy / positive regulation of protein-containing complex assembly / Hh mutants are degraded by ERAD / establishment of protein localization / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / positive regulation of non-canonical NF-kappaB signal transduction / Translesion Synthesis by POLH / ADP binding / ABC-family proteins mediated transport / autophagy / cytoplasmic stress granule / Aggrephagy / positive regulation of protein catabolic process / azurophil granule lumen / KEAP1-NFE2L2 pathway / Ovarian tumor domain proteases / positive regulation of canonical Wnt signaling pathway / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / double-strand break repair / E3 ubiquitin ligases ubiquitinate target proteins / site of double-strand break / chromosome / Neddylation / cellular response to heat / ubiquitin-dependent protein catabolic process / secretory granule lumen / protein phosphatase binding / regulation of apoptotic process / ficolin-1-rich granule lumen / proteasome-mediated ubiquitin-dependent protein catabolic process / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / membrane fusion
Similarity search - Function
Deubiquitinating protein VCPIP1 / Deubiquitinating protein VCPIP1, N-terminal / VCIP135 N-terminal / SEP domain / NSFL1 cofactor p47, SEP domain superfamily / SEP domain / SEP domain profile. / Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. / : / OTU1, UBXL domain ...Deubiquitinating protein VCPIP1 / Deubiquitinating protein VCPIP1, N-terminal / VCIP135 N-terminal / SEP domain / NSFL1 cofactor p47, SEP domain superfamily / SEP domain / SEP domain profile. / Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. / : / OTU1, UBXL domain / Domain present in ubiquitin-regulatory proteins / UBX domain / UBX domain / UBX domain profile. / UBA-like domain / OTU-like cysteine protease / OTU domain / OTU domain profile. / AAA ATPase, CDC48 family / Cell division protein 48 (CDC48), N-terminal domain / : / CDC48, N-terminal subdomain / Cell division protein 48 (CDC48) N-terminal domain / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / UBA-like superfamily / Aspartate decarboxylase-like domain superfamily / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / Ubiquitin-like domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Transitional endoplasmic reticulum ATPase / Deubiquitinating protein VCPIP1 / NSFL1 cofactor p47
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.63 Å
AuthorsShah B / Hunkeler M / Buhrlage SJ / Fischer EF
Funding support United States, 3 items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)R01 CA262188 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)R01 CA233800 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)5F31 CA281197 United States
CitationJournal: Nat Commun / Year: 2025
Title: Structural basis of VCP-VCPIP1-p47 ternary complex in Golgi maintenance.
Authors: Binita Shah / Moritz Hunkeler / Ariana Bratt / Hong Yue / Isabella Jaen Maisonet / Eric S Fischer / Sara J Buhrlage /
Abstract: VCP/p97 regulates a wide range of cellular processes, including post-mitotic Golgi reassembly. In this context, VCP is assisted by p47, an adapter protein, and VCPIP1, a deubiquitylase (DUB). ...VCP/p97 regulates a wide range of cellular processes, including post-mitotic Golgi reassembly. In this context, VCP is assisted by p47, an adapter protein, and VCPIP1, a deubiquitylase (DUB). However, how they organize into a functional ternary complex to promote Golgi assembly remains unknown. Here, we use cryo-EM to characterize both VCP-VCPIP1 and VCP-VCPIP1-p47 complexes. We show that VCPIP1 engages VCP through two interfaces: one involving the N-domain of VCP and the UBX domain of VCPIP1, and the other involving the VCP D2 domains and a region of VCPIP1 we refer to as VCPID. The p47 UBX domain competitively binds to the VCP N-domain, while not affecting VCPID binding. We show that VCPID is critical for VCP-mediated enhancement of DUB activity and proper Golgi assembly. The ternary structure along with biochemical and cellular data provides new insights into the complex interplay of VCP with its co-factors.
History
DepositionDec 31, 2024-
Header (metadata) releaseOct 15, 2025-
Map releaseOct 15, 2025-
UpdateOct 15, 2025-
Current statusOct 15, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_48504.png

Downloads & links

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Map

FileDownload / File: emd_48504.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 320 pix.
= 352. Å		1.1 Å/pix.
x 320 pix.
= 352. Å		1.1 Å/pix.
x 320 pix.
= 352. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.0661
Minimum - Maximum-0.32337993 - 0.69760585
Average (Standard dev.)-0.000517174 (±0.020901851)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 352.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_48504_msk_1.map
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Additional map: #1

Fileemd_48504_additional_1.map
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Additional map: Low pass filtered map

Fileemd_48504_additional_2.map
AnnotationLow pass filtered map
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Half map: Half-map B

Fileemd_48504_half_map_1.map
AnnotationHalf-map B
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Half map: Half-map A

Fileemd_48504_half_map_2.map
AnnotationHalf-map A
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Sample components

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Entire : Complex of valosin containing protein (VCP)/p97 bound to valosin ...

EntireName: Complex of valosin containing protein (VCP)/p97 bound to valosin containing protein interacting protein 1 (VCPIP1) and p47
Components
  • Complex: Complex of valosin containing protein (VCP)/p97 bound to valosin containing protein interacting protein 1 (VCPIP1) and p47
    • Complex: Valosin containing protein (VCP)
      • Protein or peptide: Transitional endoplasmic reticulum ATPase
    • Complex: Valosin containing protein interacting protein 1 (VCPIP1)
      • Protein or peptide: Deubiquitinating protein VCPIP1
    • Complex: p47
      • Protein or peptide: NSFL1 cofactor p47

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Supramolecule #1: Complex of valosin containing protein (VCP)/p97 bound to valosin ...

SupramoleculeName: Complex of valosin containing protein (VCP)/p97 bound to valosin containing protein interacting protein 1 (VCPIP1) and p47
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Full length valosin containing protein (VCP)/p97 with full length valosin containing protein interacting protein 1 (VCPIP1) and p47

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Supramolecule #2: Valosin containing protein (VCP)

SupramoleculeName: Valosin containing protein (VCP) / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: Valosin containing protein interacting protein 1 (VCPIP1)

SupramoleculeName: Valosin containing protein interacting protein 1 (VCPIP1)
type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: p47

SupramoleculeName: p47 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3 / Details: Adapter of valosin containing protein (VCP)/p97
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Transitional endoplasmic reticulum ATPase

MacromoleculeName: Transitional endoplasmic reticulum ATPase / type: protein_or_peptide / ID: 1 / Details: N-term FLAG-tagged VCP / Enantiomer: LEVO / EC number: vesicle-fusing ATPase
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGDYKDDDDK GGGSGGLEVL FQGPGSMASG ADSKGDDLST AILKQKNRPN RLIVDEAINE DNSVVSLSQP KMDELQLFRG DTVLLKGKKR REAVCIVLSD DTCSDEKIRM NRVVRNNLRV RLGDVISIQP CPDVKYGKRI HVLPIDDTVE GITGNLFEVY LKPYFLEAYR ...String:
MGDYKDDDDK GGGSGGLEVL FQGPGSMASG ADSKGDDLST AILKQKNRPN RLIVDEAINE DNSVVSLSQP KMDELQLFRG DTVLLKGKKR REAVCIVLSD DTCSDEKIRM NRVVRNNLRV RLGDVISIQP CPDVKYGKRI HVLPIDDTVE GITGNLFEVY LKPYFLEAYR PIRKGDIFLV RGGMRAVEFK VVETDPSPYC IVAPDTVIHC EGEPIKREDE EESLNEVGYD DIGGCRKQLA QIKEMVELPL RHPALFKAIG VKPPRGILLY GPPGTGKTLI ARAVANETGA FFFLINGPEI MSKLAGESES NLRKAFEEAE KNAPAIIFID ELDAIAPKRE KTHGEVERRI VSQLLTLMDG LKQRAHVIVM AATNRPNSID PALRRFGRFD REVDIGIPDA TGRLEILQIH TKNMKLADDV DLEQVANETH GHVGADLAAL CSEAALQAIR KKMDLIDLED ETIDAEVMNS LAVTMDDFRW ALSQSNPSAL RETVVEVPQV TWEDIGGLED VKRELQELVQ YPVEHPDKFL KFGMTPSKGV LFYGPPGCGK TLLAKAIANE CQANFISIKG PELLTMWFGE SEANVREIFD KARQAAPCVL FFDELDSIAK ARGGNIGDGG GAADRVINQI LTEMDGMSTK KNVFIIGATN RPDIIDPAIL RPGRLDQLIY IPLPDEKSRV AILKANLRKS PVAKDVDLEF LAKMTNGFSG ADLTEICQRA CKLAIRESIE SEIRRERERQ TNPSAMEVEE DDPVPEIRRD HFEEAMRFAR RSVSDNDIRK YEMFAQTLQQ SRGFGSFRFP SGNQGGAGPS QGSGGGTGGS VYTEDNDDDL YG

UniProtKB: Transitional endoplasmic reticulum ATPase

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Macromolecule #2: Deubiquitinating protein VCPIP1

MacromoleculeName: Deubiquitinating protein VCPIP1 / type: protein_or_peptide / ID: 2 / Details: N-term Strep-tagged VCPIP1 / Enantiomer: LEVO / EC number: ubiquitinyl hydrolase 1
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGDWSHPQFE KSGGGSGGLE VLFQGPGSMS QPPPPPPPLP PPPPPPEAPQ TPSSLASAAA SGGLLKRRDR RILSGSCPDP KCQARLFFPA SGSVSIECTE CGQRHEQQQL LGVEEVTDPD VVLHNLLRNA LLGVTGAPKK NTELVKVMGL SNYHCKLLSP ILARYGMDKQ ...String:
MGDWSHPQFE KSGGGSGGLE VLFQGPGSMS QPPPPPPPLP PPPPPPEAPQ TPSSLASAAA SGGLLKRRDR RILSGSCPDP KCQARLFFPA SGSVSIECTE CGQRHEQQQL LGVEEVTDPD VVLHNLLRNA LLGVTGAPKK NTELVKVMGL SNYHCKLLSP ILARYGMDKQ TGRAKLLRDM NQGELFDCAL LGDRAFLIEP EHVNTVGYGK DRSGSLLYLH DTLEDIKRAN KSQECLIPVH VDGDGHCLVH AVSRALVGRE LFWHALRENL KQHFQQHLAR YQALFHDFID AAEWEDIINE CDPLFVPPEG VPLGLRNIHI FGLANVLHRP IILLDSLSGM RSSGDYSATF LPGLIPAEKC TGKDGHLNKP ICIAWSSSGR NHYIPLVGIK GAALPKLPMN LLPKAWGVPQ DLIKKYIKLE EDGGCVIGGD RSLQDKYLLR LVAAMEEVFM DKHGIHPSLV ADVHQYFYRR TGVIGVQPEE VTAAAKKAVM DNRLHKCLLC GALSELHVPP EWLAPGGKLY NLAKSTHGQL RTDKNYSFPL NNLVCSYDSV KDVLVPDYGM SNLTACNWCH GTSVRKVRGD GSIVYLDGDR TNSRSTGGKC GCGFKHFWDG KEYDNLPEAF PITLEWGGRV VRETVYWFQY ESDSSLNSNV YDVAMKLVTK HFPGEFGSEI LVQKVVHTIL HQTAKKNPDD YTPVNIDGAH AQRVGDVQGQ ESESQLPTKI ILTGQKTKTL HKEELNMSKT ERTIQQNITE QASVMQKRKT EKLKQEQKGQ PRTVSPSTIR DGPSSAPATP TKAPYSPTTS KEKKIRITTN DGRQSMVTLK SSTTFFELQE SIAREFNIPP YLQCIRYGFP PKELMPPQAG MEKEPVPLQH GDRITIEILK SKAEGGQSAA AHSAHTVKQE DIAVTGKLSS KELQEQAEKE MYSLCLLATL MGEDVWSYAK GLPHMFQQGG VFYSIMKKTM GMADGKHCTF PHLPGKTFVY NASEDRLELC VDAAGHFPIG PDVEDLVKEA VSQVRAEATT RSRESSPSHG LLKLGSGGVV KKKSEQLHNV TAFQGKGHSL GTASGNPHLD PRARETSVVR KHNTGTDFSN SSTKTEPSVF TASSSNSELI RIAPGVVTMR DGRQLDPDLV EAQRKKLQEM VSSIQASMDR HLRDQSTEQS PSDLPQRKTE VVSSSAKSGS LQTGLPESFP LTGGTENLNT ETTDGCVADA LGAAFATRSK AQRGNSVEEL EEMDSQDAEM TNTTEPMDHS

UniProtKB: Deubiquitinating protein VCPIP1

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Macromolecule #3: NSFL1 cofactor p47

MacromoleculeName: NSFL1 cofactor p47 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHHHH HDLGTENLYF QSMMAAERQE ALREFVAVTG AEEDRARFFL ESAGWDLQIA LASFYEDGGD EDIVTISQAT PSSVSRGTAP SDNRVTSFRD LIHDQDEDEE EEEGQRFYAG GSERSGQQIV GPPRKKSPNE LVDDLFKGAK EHGAVAVERV TKSPGETSKP ...String:
MHHHHHHHHH HDLGTENLYF QSMMAAERQE ALREFVAVTG AEEDRARFFL ESAGWDLQIA LASFYEDGGD EDIVTISQAT PSSVSRGTAP SDNRVTSFRD LIHDQDEDEE EEEGQRFYAG GSERSGQQIV GPPRKKSPNE LVDDLFKGAK EHGAVAVERV TKSPGETSKP RPFAGGGYRL GAAPEEESAY VAGEKRQHSS QDVHVVLKLW KSGFSLDNGE LRSYQDPSNA QFLESIRRGE VPAELRRLAH GGQVNLDMED HRDEDFVKPK GAFKAFTGEG QKLGSTAPQV LSTSSPAQQA ENEAKASSSI LIDESEPTTN IQIRLADGGR LVQKFNHSHR ISDIRLFIVD ARPAMAATSF ILMTTFPNKE LADESQTLKE ANLLNAVIVQ RLT

UniProtKB: NSFL1 cofactor p47

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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

Concentration2 mg/mL
BufferpH: 7.4
Component:
ConcentrationNameFormula
30.0 mMHEPES
150.0 mMsodium chlorideNaCl
3.0 mMTCEP
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.039 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 283.15 K / Instrument: LEICA EM GP
DetailsFinal concentration of 0.2 mM CHAPSO

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Slit width: 10 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Number grids imaged: 1 / Number real images: 12261 / Average exposure time: 2.87 sec. / Average electron dose: 49.22 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 165000
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: 2003371
CTF correctionSoftware - Name: cryoSPARC (ver. 4.60) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionAlgorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 2.63 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.6.0) / Number images used: 463210
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.60)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.6.0)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

5ftk


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL

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