ArticleMolecular biology of the cell2013
In vivo analysis of human nucleoporin repeat domain interactions.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 37 citations in OpenAlex.
- Expandable DNA-origami rings as a nanomechanical platform for studying disordered nucleoporins.bioRxiv : the preprint server for biology · 2026Article
- FG repeats drive co-clustering of nuclear pores and P granules in the C. elegans germline.Development (Cambridge, England) · 2025Article
- The phenylalanine-and-glycine repeats of NUP98 oncofusions form condensates that selectively partition transcriptional coactivators.Molecular cell · 2025Article
- Nuclear RNA-related processes modulate the assembly of cytoplasmic RNA granules.Nucleic acids research · 2024Article
- Nucleoporin foci are stress-sensitive condensates dispensable for C. elegans nuclear pore assembly.The EMBO journal · 2023Article
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Biomolecular condensation of NUP98 fusion proteins drives leukemogenic gene expression.Nature structural & molecular biology · 2021Article
- Insight into membraneless organelles and their associated proteins: Drivers, Clients and Regulators.Computational and structural biotechnology journal · 2021Article
- The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways.Nature communications · 2020Article
- Nanocompartmentalization of the Nuclear Pore Lumen.Biophysical journal · 2020Article
- Imaging within single NPCs reveals NXF1's role in mRNA export on the cytoplasmic side of the pore.The Journal of cell biology · 2019Article
- Nuclear pores in genome architecture and enhancer function.Current opinion in cell biology · 2019Review
- A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement.ACS nano · 2018Article
- The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae.Rice (New York, N.Y.) · 2017Article
- Article
- A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics.The Journal of general physiology · 2017Article
- Metazoan Nuclear Pores Provide a Scaffold for Poised Genes and Mediate Induced Enhancer-Promoter Contacts.Molecular cell · 2017Article
- NUP98 Fusion Proteins Interact with the NSL and MLL1 Complexes to Drive Leukemogenesis.Cancer cell · 2016Article
- The selective permeability barrier in the nuclear pore complex.Nucleus (Austin, Tex.) · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The nuclear pore complex (NPC), assembled from ∼30 proteins termed nucleoporins (Nups), mediates selective nucleocytoplasmic trafficking. A subset of nucleoporins bear a domain with multiple phenylalanine-glycine (FG) motifs. As binding sites for transport receptors, FG Nups are critical in translocation through the NPC. Certain FG Nups are believed to associate via low-affinity, cohesive interactions to form the permeability barrier of the pore, although the form and composition of this functional barrier are debated. We used green fluorescent protein-Nup98/HoxA9 constructs with various numbers of repeats and also substituted FG domains from other nucleoporins for the Nup98 domain to directly compare cohesive interactions in live cells by fluorescence recovery after photobleaching (FRAP). We find that cohesion is a function of both number and type of FG repeats. Glycine-leucine-FG (GLFG) repeat domains are the most cohesive. FG domains from several human nucleoporins showed no interactions in this assay; however, Nup214, with numerous VFG motifs, displayed measurable cohesion by FRAP. The cohesive nature of a human nucleoporin did not necessarily correlate with that of its yeast orthologue. The Nup98 GLFG domain also functions in pore targeting through binding to Nup93, positioning the GLFG domain in the center of the NPC and supporting a role for this nucleoporin in the permeability barrier.
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Registered trials
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.