Comprehensive structure and functional adaptations of the yeast nuclear pore complex
Open accessPublished version of a preprint
Abstract
Nuclear pore complexes (NPCs) mediate the nucleocytoplasmic transport of macromolecules. Here we provide a structure of the isolated yeast NPC in which the inner ring is resolved by cryo-EM at sub-nanometer resolution to show how flexible connectors tie together different structural and functional layers. These connectors may be targets for phosphorylation and regulated disassembly in cells with an open mitosis. Moreover, some nucleoporin pairs and transport factors have similar interaction motifs, which suggests an evolutionary and mechanistic link between assembly and transport. We provide evidence for three major NPC variants that may foreshadow functional specializations at the nuclear periphery. Cryo-electron tomography extended these studies, providing a model of the in situ NPC with a radially expanded inner ring. Our comprehensive model reveals features of the nuclear basket and central transporter, suggests a role for the lumenal Pom152 ring in restricting dilation, and highlights structural plasticity that may be required for transport.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold
Fontana, P., Dong, Y., Pi, X., Tong, A. B., Hecksel, C. W., Wang, L., Fu, T.-M., Bustamante, C., & Wu, H. (2022) · Science · doi:10.1126/science.abm9326 · Cited by 195 · see citing works
- Authors
- Akey, C. W., Singh, D., Ouch, C., Echeverria, I., Nudelman, I., Varberg, J. M., Yu, Z., Fang, F., Shi, Y., Wang, J., Salzberg, D., Song, K., Xu, C., Gumbart, J. C., Suslov, S., Unruh, J., Jaspersen, S. L., Chait, B. T., Sali, A., Fernandez-Martinez, J., Ludtke, S. J., Villa, E., & Rout, M. P.
- Affiliations
- Boston University (US)
- University of California San Diego (US)
- University of California, San Francisco (US)
- Rockefeller University (US)
- Stowers Institute for Medical Research (US)
- University of Pittsburgh (US)
- University of Massachusetts Chan Medical School (US)
- Georgia Institute of Technology (US)
- Baylor College of Medicine (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Akey, Christopher W.
- Ludtke, Steven J.
- Villa, Elizabeth
- Rout, Michael P.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2022-01
- Volume
- 185
- Issue
- 2
- Pages
- 361-378.e25
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC8928745
- OpenAlex
- W4220942300
- Cited by
- 180
- References
- 1
- Citations by year
- 2026: 18 · 2025: 33 · 2024: 41 · 2023: 48 · 2022: 39 · 2021: 1
- FWCI
- 13.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by-nc-nd)
- Digital Commons-TMC (Texas Medical Center) (submittedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by-nc-nd)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc-nd)
- Funders
- Howard Hughes Medical Institute
- PEW Charitable Trusts
- Damon Runyon Cancer Research Foundation
- NSF
- Israel National Road Safety Authority
- National Institutes of Health (DP2 GM123494, F32 GM133096, NSF-1818129, P01 GM121203, P41 GM109824, R01 GM112108, R01 GM117212, R01 GM121443, R01 GM45377)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- nuclear pore complex, nuclear transport, yeast, nucleoporins, nuclear basket, open mitosis, phosphorylation, cryo-electron tomography, structural plasticity
- MeSH terms
- Protein Domains, Adaptation, Physiological, Amino Acid Sequence, Fluorescence, Nuclear Envelope, Saccharomyces cerevisiae, Reproducibility of Results, Amino Acid Motifs, Nuclear Pore, Nuclear Pore Complex Proteins, Saccharomyces cerevisiae Proteins, Molecular Docking Simulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review