nuclear pore transmembrane ring / protein localization to nuclear inner membrane / nuclear pore inner ring / nuclear pore central transport channel / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore complex assembly / nuclear pore organization / structural constituent of nuclear pore / nuclear localization sequence binding / NLS-bearing protein import into nucleus ...nuclear pore transmembrane ring / protein localization to nuclear inner membrane / nuclear pore inner ring / nuclear pore central transport channel / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore complex assembly / nuclear pore organization / structural constituent of nuclear pore / nuclear localization sequence binding / NLS-bearing protein import into nucleus / RNA export from nucleus / nucleocytoplasmic transport / poly(A)+ mRNA export from nucleus / mRNA transport / nuclear pore / nuclear periphery / phospholipid binding / protein import into nucleus / protein transport / nuclear membrane / protein-macromolecule adaptor activity / cytosol Similarity search - Function
National Natural Science Foundation of China (NSFC)
China
Citation
Journal: Cell Res / Year: 2022 Title: Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex. Authors: Gaoxingyu Huang / Xiechao Zhan / Chao Zeng / Ke Liang / Xuechen Zhu / Yanyu Zhao / Pan Wang / Qifan Wang / Qiang Zhou / Qinghua Tao / Minhao Liu / Jianlin Lei / Chuangye Yan / Yigong Shi / Abstract: Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy structure of the inner ring (IR) subunit from the Xenopus laevis NPC at an ...Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy structure of the inner ring (IR) subunit from the Xenopus laevis NPC at an average resolution of 4.2 Å. A homo-dimer of Nup205 resides at the center of the IR subunit, flanked by two molecules of Nup188. Four molecules of Nup93 each places an extended helix into the axial groove of Nup205 or Nup188, together constituting the central scaffold. The channel nucleoporin hetero-trimer of Nup62/58/54 is anchored on the central scaffold. Six Nup155 molecules interact with the central scaffold and together with the NDC1-ALADIN hetero-dimers anchor the IR subunit to the nuclear envelope and to outer rings. The scarce inter-subunit contacts may allow sufficient latitude in conformation and diameter of the IR. Our structure reveals the molecular basis for the IR subunit assembly of a vertebrate NPC.
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