ArticleMolecular biology of the cell1998
A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- Nuclear envelope budding and its cellular functions.Nucleus (Austin, Tex.) · 2023Article
- Uip4p modulates nuclear pore complex function inNucleus (Austin, Tex.) · 2022Article
- Nuclear envelope-vacuole contacts mitigate nuclear pore complex assembly stress.The Journal of cell biology · 2020Article
- Fantastic nuclear envelope herniations and where to find them.Biochemical Society transactions · 2018Review
- A novel function for the Caenorhabditis elegans torsin OOC-5 in nucleoporin localization and nuclear import.Molecular biology of the cell · 2015Article
- Time-course proteome analysis reveals the dynamic response of Cryptococcus gattii cells to fluconazole.PloS one · 2012Article
- Members of the RSC chromatin-remodeling complex are required for maintaining proper nuclear envelope structure and pore complex localization.Molecular biology of the cell · 2010Article
- ER membrane-bending proteins are necessary for de novo nuclear pore formation.The Journal of cell biology · 2009Article
- Mutations affecting spindle pole body and mitotic exit network function are synthetically lethal with a deletion of the nucleoporin NUP1 in S. cerevisiae.Current genetics · 2008Article
- Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport.The Journal of cell biology · 2007Article
- The karyopherin Kap95 regulates nuclear pore complex assembly into intact nuclear envelopes in vivo.Molecular biology of the cell · 2007Article
- Article
- Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.Molecular biology of the cell · 2005Article
- Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization.Eukaryotic cell · 2005Article
- A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role for the spindle pole body component Ndc1p in nuclear pore assembly.Eukaryotic cell · 2004Article
- Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans.Molecular biology of the cell · 2003Article
- Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating.Molecular and cellular biology · 2003Article
- Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly.BMC genetics · 2002Article
- The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport.Molecular and cellular biology · 2001Article
- Perturbation of the nucleus: a novel Hog1p-independent, Pkc1p-dependent consequence of hypertonic shock in yeast.Molecular biology of the cell · 2001Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes (NPCs) are large proteinaceous portals for exchanging macromolecules between the nucleus and the cytoplasm. Revealing how this transport apparatus is assembled will be critical for understanding the nuclear transport mechanism. To address this issue and to identify factors that regulate NPC formation and dynamics, a novel fluorescence-based strategy was used. This approach is based on the functional tagging of NPC proteins with the green fluorescent protein (GFP), and the hypothesis that NPC assembly mutants will have distinct GFP-NPC signals as compared with wild-type (wt) cells. By fluorescence-activated cell sorting for cells with low GFP signal from a population of mutagenized cells expressing GFP-Nup49p, three complementation groups were identified: two correspond to mutant nup120 and gle2 alleles that result in clusters of NPCs. Interestingly, a third group was a novel temperature-sensitive allele of nup57. The lowered GFP-Nup49p incorporation in the nup57-E17 cells resulted in a decreased fluorescence level, which was due in part to a sharply diminished interaction between the carboxy-terminal truncated nup57pE17 and wt Nup49p. Interestingly, the nup57-E17 mutant also affected the incorporation of a specific subset of other nucleoporins into the NPC. Decreased levels of NPC-associated Nsp1p and Nup116p were observed. In contrast, the localizations of Nic96p, Nup82p, Nup159p, Nup145p, and Pom152p were not markedly diminished. Coincidentally, nuclear import capacity was inhibited. Taken together, the identification of such mutants with specific perturbations of NPC structure validates this fluorescence-based strategy as a powerful approach for providing insight into the mechanism of NPC biogenesis.
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