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12DL

Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs

This is a non-PDB format compatible entry.
Summary for 12DL
Entry DOI10.2210/pdb12dl/pdb
EMDB information76334
DescriptorTubulin beta-4B chain, NACHT, LRR and PYD domains-containing protein 14, E3 ubiquitin-protein ligase UHRF1, ... (20 entities in total)
Functional Keywordscytoplasmic lattice, egg, filamentous assembly, cytosolic protein
Biological sourceMus musculus (house mouse)
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Total number of polymer chains33
Total formula weight2137881.17
Authors
Li, Y.,Zheng, W.,Leem, J.,Wu, C.,Tang, S.,Mogessie, B.,Xiong, Y. (deposition date: 2026-03-29, release date: 2026-04-08, Last modification date: 2026-07-29)
Primary citationLi, Y.,Zheng, W.,Leem, J.,Wu, C.,Tang, S.,Mogessie, B.,Xiong, Y.
Cytoplasmic lattices store developmentally poised degradative and cytoskeletal complexes in mammalian eggs.
Nat.Struct.Mol.Biol., 2026
Cited by
PubMed Abstract: The cytoplasmic lattice (CPL) in mammalian eggs is essential for early embryonic development but its molecular components, structural organization and functional capacity have remained elusive. Here, using cryo-electron microscopy, we show that the CPL filament in mouse metaphase II eggs contains repeating units with a periodicity of ~37 nm and determine its high-resolution, native structure and complete subunit composition. The CPL architecture organizes maternal-effect proteins, ubiquitination machinery and tubulin into a highly structured reservoir. Maternal-effect proteins form the scaffold of the CPL to sequester a UHRF1-UBE2D3 E3-E2 ubiquitination module and three distinct FBXW-SKP1 E3 ubiquitin ligase components, notably all in activity-excluded states. The CPL further contains αβ-tubulin heterodimers in a GTP-bound state, indicating microtubule-assembly-competent tubulin held in reserve. CPL filaments are capped by a terminal unit that lacks a PADI6 dimer, a scaffold component, suggesting a structural mechanism that prevents further oligomerization. Interactions between neighboring CPL filaments promote the assembly of a three-dimensional network in the egg cytoplasm. Taken together, our work defines how CPL assembly and architecture prime mammalian eggs for ubiquitin-mediated protein degradation and cytoskeletal remodeling during the egg-to-embryo transition.
PubMed: 42426369
DOI: 10.1038/s41594-026-01843-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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PDB entries from 2026-09-09

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