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Published December 2022 | public
Journal Article

Structure and Function of the Nuclear Pore Complex


The nucleus, a genome-containing organelle eponymous of eukaryotes, is enclosed by a double membrane continuous with the endoplasmic reticulum. The nuclear pore complex (NPC) is an ∼110-MDa, ∼1000-protein channel that selectively transports macromolecules across the nuclear envelope and thus plays a central role in the regulated flow of genetic information from transcription to translation. Its size, complexity, and flexibility have hindered determination of atomistic structures of intact NPCs. Recent studies have overcome these hurdles by combining biochemical reconstitution and docking of high-resolution structures of NPC subcomplexes into cryo-electron tomographic reconstructions with biochemical and physiological validation. Here, we provide an overview of the near-atomic composite structure of the human NPC, a milestone toward unlocking a molecular understanding of mRNA export, NPC-associated diseases, and viral host–pathogen interactions, serving as a paradigm for studying similarly large complexes.

Additional Information

We apologize to the colleagues whose work could not be adequately discussed because of the length constraint of this review. We thank all current and former members of the Hoelz laboratory for the drive, tenacity, and acumen that have made the laboratory's contributions to the nucleocytoplasmic transport field possible; Ana Correia for her insight into nucleoporin diseases; and Valerie Altounian for the preparation of the NPC schematic. A.H. is a Faculty Scholar of the Howard Hughes Medical Institute and was supported by National Institutes of Health Grants R01-GM111461 and R01-GM117360.

Additional details

August 22, 2023
December 22, 2023