ArticleMolecular & cellular proteomics : MCP2014
Integrative structure-function mapping of the nucleoporin Nup133 suggests a conserved mechanism for membrane anchoring of the nuclear pore complex.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Evolutionary, structural and functional insights in nuclear organisation and nucleocytoplasmic transport in trypanosomes.FEBS letters · 2023Review
- Implications of a multiscale structure of the yeast nuclear pore complex.Molecular cell · 2023Article
- Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane.The Journal of cell biology · 2023Article
- Quality control mechanisms that protect nuclear envelope identity and function.The Journal of cell biology · 2022Review
- Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold.Science (New York, N.Y.) · 2022Article
- Integration of software tools for integrative modeling of biomolecular systems.Journal of structural biology · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- On the nuclear pore complex and its emerging role in cellular mechanotransduction.APL bioengineering · 2022Review
- Article
- Targeted Cross-Linking Mass Spectrometry on Single-Step Affinity Purified Molecular Complexes in the Yeast Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex.Trends in biochemical sciences · 2021Review
- Regulation of diverse nuclear shapes: pathways working independently, together.Communicative & integrative biology · 2021Review
- A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure.Nature communications · 2020Article
- Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif.Nature communications · 2020Article
- PinX1t, a Novel PinX1 Transcript Variant, Positively Regulates Cardiogenesis of Embryonic Stem Cells.Journal of the American Heart Association · 2020Article
- Federating Structural Models and Data: Outcomes from A Workshop on Archiving Integrative Structures.Structure (London, England : 1993) · 2019Article
- Archiving and disseminating integrative structure models.Journal of biomolecular NMR · 2019Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
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16 authors.
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Abstract
The nuclear pore complex (NPC) is the sole passageway for the transport of macromolecules across the nuclear envelope. Nup133, a major component in the essential Y-shaped Nup84 complex, is a large scaffold protein of the NPC's outer ring structure. Here, we describe an integrative modeling approach that produces atomic models for multiple states of Saccharomyces cerevisiae (Sc) Nup133, based on the crystal structures of the sequence segments and their homologs, including the related Vanderwaltozyma polyspora (Vp) Nup133 residues 55 to 502 (VpNup133(55-502)) determined in this study, small angle X-ray scattering profiles for 18 constructs of ScNup133 and one construct of VpNup133, and 23 negative-stain electron microscopy class averages of ScNup133(2-1157). Using our integrative approach, we then computed a multi-state structural model of the full-length ScNup133 and validated it with mutational studies and 45 chemical cross-links determined via mass spectrometry. Finally, the model of ScNup133 allowed us to annotate a potential ArfGAP1 lipid packing sensor (ALPS) motif in Sc and VpNup133 and discuss its potential significance in the context of the whole NPC; we suggest that ALPS motifs are scattered throughout the NPC's scaffold in all eukaryotes and play a major role in the assembly and membrane anchoring of the NPC in the nuclear envelope. Our results are consistent with a common evolutionary origin of Nup133 with membrane coating complexes (the protocoatomer hypothesis); the presence of the ALPS motifs in coatomer-like nucleoporins suggests an ancestral mechanism for membrane recognition present in early membrane coating complexes.
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