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Open data
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Basic information
| Entry | Database: PDB / ID: 9xrl | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Structure of mouse cytoplasmic lattice (CPL) repeating unit | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components |
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Keywords | CYTOSOLIC PROTEIN / cytoplasmic lattice / maternal effect protein / proteostasis / protein storage | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of translation by machinery localization / Prolactin receptor signaling / Signaling by BMP / subcortical maternal complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / establishment of organelle localization / Chromatin modifying enzymes / protein storage ...regulation of translation by machinery localization / Prolactin receptor signaling / Signaling by BMP / subcortical maternal complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / establishment of organelle localization / Chromatin modifying enzymes / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / cortical granule exocytosis / embryonic process involved in female pregnancy / endoplasmic reticulum localization / ooplasm / Carboxyterminal post-translational modifications of tubulin / Intraflagellar transport / establishment or maintenance of apical/basal cell polarity / SCF-beta-TrCP mediated degradation of Emi1 / COPI-independent Golgi-to-ER retrograde traffic / E3 ubiquitin ligases ubiquitinate target proteins / Downregulation of SMAD2/3:SMAD4 transcriptional activity / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / cytoplasm organization / Regulation of BACH1 activity / histone H3K18 ubiquitin ligase activity / histone H3K14 ubiquitin ligase activity / histone H3 ubiquitin ligase activity / PINK1-PRKN Mediated Mitophagy / Inactivation of CSF3 (G-CSF) signaling / SCF(Skp2)-mediated degradation of p27/p21 / histone H3K23 ubiquitin ligase activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / COPI-mediated anterograde transport / spermatogonial cell division / Regulation of TNFR1 signaling / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Kinesins / histone H3 reader activity / Regulation of RUNX2 expression and activity / cortical granule / Degradation of GLI1 by the proteasome / Cyclin D associated events in G1 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / IKK complex recruitment mediated by RIP1 / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Dectin-1 mediated noncanonical NF-kB signaling / NIK-->noncanonical NF-kB signaling / PKR-mediated signaling / Aggrephagy / RHO GTPases activate IQGAPs / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / Degradation of beta-catenin by the destruction complex / Activation of NF-kappaB in B cells / Recycling pathway of L1 / Iron uptake and transport / The role of GTSE1 in G2/M progression after G2 checkpoint / COPI-dependent Golgi-to-ER retrograde traffic / apical cortex / positive regulation of meiotic nuclear division / regulation of RNA stability / positive regulation of embryonic development / chromosomal DNA methylation maintenance following DNA replication / FCERI mediated NF-kB activation / axonemal microtubule / CLEC7A (Dectin-1) signaling / Interleukin-1 signaling / Hedgehog 'off' state / RHO GTPases Activate Formins / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / F-box domain binding / organelle transport along microtubule / Anchoring of the basal body to the plasma membrane / Separation of Sister Chromatids / Downstream TCR signaling / Recruitment of NuMA to mitotic centrosomes / AURKA Activation by TPX2 / hemi-methylated DNA-binding / regulation of establishment of protein localization / forebrain morphogenesis / Peroxisomal protein import / GLI3 is processed to GLI3R by the proteasome / PcG protein complex / cerebellar cortex morphogenesis / Regulation of PLK1 Activity at G2/M Transition / Neddylation / glial cell differentiation / neuron projection arborization / dentate gyrus development / embryonic pattern specification / (E3-independent) E2 ubiquitin-conjugating enzyme / mitochondrion localization / establishment of spindle localization Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.74 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Chi, P.L. / Wang, X. / Li, J.L. / Deng, D. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Nature / Year: 2026Title: Structure of the mouse cytoplasmic lattice. Authors: Pengliang Chi / Xiang Wang / Jialu Li / Jingrui Huang / Sicheng Ju / Sibei Liu / Li Yan / Yuechao Lu / Zihan Zhang / Zhuo Han / Jinhong Li / Qianqian Qi / Qingting Liu / Yiren Zeng / Li Guo ...Authors: Pengliang Chi / Xiang Wang / Jialu Li / Jingrui Huang / Sicheng Ju / Sibei Liu / Li Yan / Yuechao Lu / Zihan Zhang / Zhuo Han / Jinhong Li / Qianqian Qi / Qingting Liu / Yiren Zeng / Li Guo / Xiaofeng Zhang / Long Gui / Dong Deng / ![]() Abstract: The fertilized egg relies almost entirely on maternal stores in the oocyte to ensure the successful initiation of development. The cytoplasmic lattices (CPLs) in mammalian oocytes store maternal- ...The fertilized egg relies almost entirely on maternal stores in the oocyte to ensure the successful initiation of development. The cytoplasmic lattices (CPLs) in mammalian oocytes store maternal-expressed proteins and have an essential role in embryogenesis. Impairing multiple CPL members leads to early embryonic arrest, resulting in infertility in mammals. However, the mechanism underlying the assembly and storage of CPLs remains largely unknown. Here we report the cryo-electron microscopy structure of a native mouse CPL repeating unit (approximately 4 MDa) at 3.74 Å resolution. This repeating unit exhibits a tripartite architecture comprising a framework, extended linkers and a CPL core. The external framework is built from PADI6 decamers and the subcortical maternal complexes. Two linkers formed by NLRP4F polymerize the frameworks into an extended filament. In the CPL core, the epigenetic regulator UHRF1 is trapped by PADI6, UBE2D and NLRP14 in a compact, autoinhibited conformation that prevents nuclear entry and ubiquitin ligase activity. Moreover, the CPL core stores GTP-bound α/β-tubulin heterodimers and inactive SCF E3-ubiquitin ligase components (FBXW-SKP1 complex) in a poised but restrained state. These features establish CPLs as a dynamic regulatory pool that enables rapid microtubule assembly and tightly controlled ubiquitination during the oocyte-to-embryo transition. Together, this semi-in situ structure illuminates CPL assembly and storage-module organization, and establishes CPLs as specialized proteostasis organelles for maternal regulation in oocytes and early embryonic development. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9xrl.cif.gz | 6.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9xrl.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9xrl.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xr/9xrl ftp://data.pdbj.org/pub/pdb/validation_reports/xr/9xrl | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 67147MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 12 types, 61 molecules 13946AADpOqFEIzPAC8HQihSTYbXZVWn...
| #1: Protein | Mass: 25643.373 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 48055.301 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 18693.992 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 65187.332 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 108001.281 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 76854.109 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 18481.295 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 54205.703 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 49877.824 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 50188.441 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P68369, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement #14: Protein | Mass: 16706.133 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P61079, E2 ubiquitin-conjugating enzyme, (E3-independent) E2 ubiquitin-conjugating enzyme #15: Protein | Mass: 88436.805 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-F-box and WD-40 domain protein ... , 2 types, 3 molecules ALC
| #3: Protein | Mass: 54517.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #16: Protein | Mass: 53657.457 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
-NACHT, LRR and PYD domains-containing protein ... , 2 types, 9 molecules yAB0752wAKAQ
| #11: Protein | Mass: 119819.859 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 113527.188 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 4 types, 25 molecules 






| #17: Chemical | ChemComp-ZN / #18: Chemical | ChemComp-GTP / #19: Chemical | ChemComp-MG / #20: Chemical | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: mouse cytoplasmic lattice / Type: COMPLEX / Entity ID: #1-#7, #9-#10, #8, #11-#16 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 6.7 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | |||||||||
| 3D reconstruction | Resolution: 3.74 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 349408 / Symmetry type: POINT | |||||||||
| Refinement | Cross valid method: NONE |
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FIELD EMISSION GUN