近日，西湖大学施一公、黄高兴宇等研究人员合作揭示非洲爪蟾核孔复合体（NPC）的细胞质环结构。2022年6月10日出版的《科学》发表了这项成果。

NPC介导核细胞质货物的运输。研究人员提出了一个单粒子的冷冻电镜重建，在3.7-4.7埃的分辨率下，重建了来自非洲爪蟾NPC的细胞质环（CR）亚单位。Nup358的一个氨基末端结构域的结构已经在3.0埃的分辨率下被解析出来，促进了每个CR亚单位中五个Nup358分子的识别。

最终的CR亚单位模型包括五个Nup358、两个Nup205和两个Nup93分子，此外还有两个先前表征的Y复合体。Nup160的羧基端片段在每个Y复合物的顶点作为一个组织中心。结构分析显示了Nup93、Nup205和Nup358如何促进和加强主要由两层Y复合体形成的CR支架组装。

附：英文原文

Title: Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex

Author: Xuechen Zhu, Gaoxingyu Huang, Chao Zeng, Xiechao Zhan, Ke Liang, Qikui Xu, Yanyu Zhao, Pan Wang, Qifan Wang, Qiang Zhou, Qinghua Tao, Minhao Liu, Jianlin Lei, Chuangye Yan, Yigong Shi

Issue&Volume: 2022-06-10

Abstract: The nuclear pore complex (NPC) mediates nucleocytoplasmic cargo transport. Here, we present a single-particle cryo–electron microscopy reconstruction of the cytoplasmic ring (CR) subunit from the Xenopus laevis NPC at 3.7- to 4.7-angstrom resolution. The structure of an amino-terminal domain of Nup358 has been resolved at 3.0 angstroms, facilitating the identification of five Nup358 molecules in each CR subunit. Our final model of the CR subunit included five Nup358, two Nup205, and two Nup93 molecules in addition to the two previously characterized Y complexes. The carboxyl-terminal fragment of Nup160 served as an organizing center at the vertex of each Y complex. Structural analysis revealed how Nup93, Nup205, and Nup358 facilitate and strengthen the assembly of the CR scaffold that is primarily formed by two layers of Y complexes.

DOI: abl8280

Source: https://www.science.org/doi/10.1126/science.abl8280