The Structure of the Nuclear Pore Complex (An Update)
- Creators
- Lin, Daniel H.
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Hoelz, André
Abstract
The nuclear pore complex (NPC) serves as the sole bidirectional gateway of macromolecules in and out of the nucleus. Owing to its size and complexity (∼1,000 protein subunits, ∼110 MDa in humans), the NPC has remained one of the foremost challenges for structure determination. Structural studies have now provided atomic-resolution crystal structures of most nucleoporins. The acquisition of these structures, combined with biochemical reconstitution experiments, cross-linking mass spectrometry, and cryo–electron tomography, has facilitated the determination of the near-atomic overall architecture of the symmetric core of the human, fungal, and algal NPCs. Here, we discuss the insights gained from these new advances and outstanding issues regarding NPC structure and function. The powerful combination of bottom-up and top-down approaches toward determining the structure of the NPC offers a paradigm for uncovering the architectures of other complex biological machines to near-atomic resolution.
Additional Information
© 2019 Annual Reviews. Review in Advance first posted on March 18, 2019. The authors are not aware of any affiliations, memberships, funding, or financial holdings that might be perceived as affecting the objectivity of this review. We apologize to our colleagues whose work was not discussed adequately owing to space constraints. We thank all current and former members of the Hoelz laboratory for their dedication, insight, and camaraderie, which have made our laboratory's contributions to the advances in NPC structure possible; Ferdinand Huber, George Mobbs, Si Nie, Alina Patke, and Stefan Petrovic for critical reading of the manuscript; and Valerie Altounian for the preparation of the animations and NPC schematics. We acknowledge Martin Beck for sharing the C. reinhardtii NPC cryo-ET reconstruction prior to publication for production of figures. A.H. is an Investigator of the Heritage Medical Research Institute and a Faculty Scholar of the Howard Hughes Medical Institute and was supported by National Institutes of Health grants R01-GM111461 and R01-GM117360 and a Camille Dreyfus Teacher-Scholar Award from the Camille and Henry Dreyfus Foundation.Attached Files
Accepted Version - nihms-1027341.pdf
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Additional details
- PMCID
- PMC6588426
- Eprint ID
- 94119
- Resolver ID
- CaltechAUTHORS:20190325-111006962
- Heritage Medical Research Institute
- Howard Hughes Medical Institute (HHMI)
- R01-GM111461
- NIH
- R01-GM117360
- NIH
- Camille and Henry Dreyfus Foundation
- Created
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2019-03-25Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field
- Caltech groups
- Heritage Medical Research Institute