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Cell Res June 1, 2020; 30 (6): 532-540.
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Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex.

Zhang Y , Li S , Zeng C , Huang G , Zhu X , Wang Q , Wang K , Zhou Q , Yan C , Zhang W , Yang G , Liu M , Tao Q , Lei J , Shi Y .

The nuclear pore complex (NPC) mediates the flow of substances between the nucleus and cytoplasm in eukaryotic cells. Here we report the cryo-electron tomography (cryo-ET) structure of the luminal ring (LR) of the NPC from Xenopus laevis oocyte. The observed key structural features of the LR are independently confirmed by single-particle cryo-electron microscopy (cryo-EM) analysis. The LR comprises eight butterfly-shaped subunits, each containing two symmetric wings. Each wing consists of four elongated, tubular protomers. Within the LR subunit, the eight protomers form a Finger domain, which directly contacts the fusion between the inner and outer nuclear membranes and a Grid domain, which serves as a rigid base for the Finger domain. Two neighboring LR subunits interact with each other through the lateral edges of their wings to constitute a Bumper domain, which displays two major conformations and appears to cushion neighboring NPCs. Our study reveals previously unknown features of the LR and potentially explains the elastic property of the NPC.

PubMed ID: 32367042
PMC ID: PMC7264284
Article link: Cell Res
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: elavl2 emd grap2 kidins220 mcf2l.2 ndc1 nup210 psmd6 pycard sult2a1

Article Images: [+] show captions
References [+] :
Akey, Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. 1993, Pubmed, Xenbase