ArticleNature communications2020
Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 43 citations in OpenAlex.
- Screening of amphipathic helices identifies features linked to inner nuclear membrane properties.Nature communications · 2026Article
- Membrane curvature elastic stress triggers recruitment of PML-II onto the inner nuclear membrane.Molecular biology of the cell · 2026Article
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Targeting colorectal cancer at the level of nuclear pore complex.Journal of advanced research · 2025Review
- A noncanonical GTPase signaling mechanism controls exit from mitosis in budding yeast.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Nuclear basket proteins regulate the distribution and mobility of nuclear pore complexes in budding yeast.Molecular biology of the cell · 2024Article
- Docking a flexible basket onto the core of the nuclear pore complex.Nature cell biology · 2024Article
- A noncanonical GTPase signaling mechanism controls exit from mitosis in budding yeast.bioRxiv : the preprint server for biology · 2024Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Lipid packing in biological membranes governs protein localization and membrane permeability.Biophysical journal · 2023Article
- Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane.The Journal of cell biology · 2023Article
- The scaffold nucleoporins SAR1 and SAR3 are essential for proper meiotic progression inFrontiers in cell and developmental biology · 2023Article
- Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022Review
- Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold.Science (New York, N.Y.) · 2022Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Review
- Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex.Cell research · 2022Article
- The endophilin curvature-sensitive motif requires electrostatic guidance to recycle synaptic vesicles in vivo.Developmental cell · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The hallmark of the eukaryotic cell is the complex endomembrane system that compartmentalizes cellular functions. Transport into and out of the nucleus occurs through the nuclear pore complex (NPC). The heptameric Nup84 or Y complex is an essential scaffolding component of the NPC. Here we report two nanobody-bound structures: the full-length Nup84-Nup133 C-terminal domain complex and the Nup133 N-terminal domain, both from S. cerevisiae. Together with previously published structures, this work enables the structural description of the entire 575 kDa Y complex from one species. The structure of Nup84-Nup133
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.