期刊
SCIENCE
卷 350, 期 6256, 页码 56-64出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aac9176
关键词
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资金
- National Cancer Institute [ACB-12002]
- National Institute of General Medical Sciences [AGM-12006]
- Deutsche Forschungsgemeinschaft
- Caltech-Amgen Research Collaboration
- Boehringer Ingelheim Fonds
- NIH [R01-GM090324, U54-GM087519, U01-GM094588, R01-GM111461]
- University of Chicago Comprehensive Cancer Center [P30-CA014599]
- Searle Funds at The Chicago Community Trust
- Caltech
- V Foundation for Cancer Research
- Edward Mallinckrodt Jr. Foundation
- Sidney Kimmel Foundation for Cancer Research
- Camille and Henry Dreyfus Foundation
The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the similar to 425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1.Nup49.Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT.Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.
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