ArticleThe Journal of cell biology1995
The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 210 citations in OpenAlex.
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Dynamic Organellar Mapping in yeast reveals extensive protein localization changes during ER stress.Nature communications · 2025Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Structural basis for the midnolin-proteasome pathway and its role in suppressing myeloma.Molecular cell · 2025Article
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024Review
- Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.Nature communications · 2023Article
- A simple thermodynamic description of phase separation of Nup98 FG domains.Nature communications · 2022Article
- Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex.Nature communications · 2022Article
- Atomic resolution dynamics of cohesive interactions in phase-separated Nup98 FG domains.Nature communications · 2022Article
- On the role of phase separation in the biogenesis of membraneless compartments.The EMBO journal · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Using Single Molecule RNA FISH to Determine Nuclear Export and Transcription Phenotypes in Drosophila Tissues.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Recapitulation of selective nuclear import and export with a perfectly repeated 12mer GLFG peptide.Nature communications · 2021Article
- Article
- Nuclear envelope-vacuole contacts mitigate nuclear pore complex assembly stress.The Journal of cell biology · 2020Article
- Mechanisms of nuclear mRNA export: A structural perspective.Traffic (Copenhagen, Denmark) · 2019Review
- Calcium Regulates the Nuclear Localization of Protein Arginine Deiminase 2.Biochemistry · 2019Article
- The Effect of FG-Nup Phosphorylation on NPC Selectivity: A One-Bead-Per-Amino-Acid Molecular Dynamics Study.International journal of molecular sciences · 2019Article
- A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement.ACS nano · 2018Article
- Article
42 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Nup116p is a member of a family of five yeast nuclear pore complex (NPC) proteins that share an amino terminal region of repetitive tetrapeptide "GLFG" motifs. Previous experiments characterized the unique morphological perturbations that occur in a nup116 null mutant: temperature-sensitive formation of nuclear envelope seals over the cytoplasmic face of the NPC (Wente, S. R., and G. Blobel. 1993. J. Cell Biol. 123:275-284). Three approaches have been taken to dissect the structural basis for Nup116p's role in NPC function. First, deletion mutagenesis analysis of NUP116 revealed that the GLFG region was required for NPC function. This was not true for the other four yeast GLFG family members (Nup49p, Nup57p, Nup100p, and Nup145p). Moreover, deletion of either half of Nup116p's GLFG repeats or replacement of Nup116p's GLFG region with either Nup100p's GLFG region or Nsp1p's FXFG repetitive region abolishes the function of Nup116p. At a semipermissive growth temperature, the cells lacking Nup116p's GLFG region displayed a diminished capacity for nuclear import. Second, overexpression of Nup116p's GLFG region severely inhibited cell growth, rapidly blocked polyadenylated-RNA export, and fragmented the nucleolus. Although it inhibited nuclear export, the overexpressed GLFG region appeared predominantly localized in the cytoplasm and NPC/nuclear envelope structure was not perturbed in thin section electron micrographs. Finally, using biochemical and two-hybrid analysis, an interaction was characterized between Nup116p's GLFG region and Kap95p, an essential yeast homologue of the vertebrate nuclear import factor p97/Imp90/karopherin beta. These data show that Nup116p's GLFG region has an essential role in mediating nuclear transport.
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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.