Journal
NATURE
Volume 555, Issue 7697, Pages 475-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature26003
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Funding
- NSF [GRF 1650113, CHE-1531823]
- SIMR
- NIH [R01 GM080477, U54 GM103511, R01 GM112108, P41 GM109824, P50 GM076547, R01 GM063834, R01 GM080139, P41 GM103314, R01 GM083960, U54 DK107981]
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Nuclear pore complexes play central roles as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm. However, their large size and dynamic nature have impeded a full structural and functional elucidation. Here we determined the structure of the entire 552-protein nuclear pore complex of the yeast Saccharomyces cerevisiae at sub-nanometre precision by satisfying a wide range of data relating to the molecular arrangement of its constituents. The nuclear pore complex incorporates sturdy diagonal columns and connector cables attached to these columns, imbuing the structure with strength and flexibility. These cables also tie together all other elements of the nuclear pore complex, including membrane-interacting regions, outer rings and RNA-processing platforms. Inwardly directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized into distinct functional units. This integrative structure enables us to rationalize the architecture, transport mechanism and evolutionary origins of the nuclear pore complex.
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