ArticleMolecular and cellular biology1996
Yeast N1e3p/Nup170p is required for normal stoichiometry of FG nucleoporins within the nuclear pore complex.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 50 citations in OpenAlex.
- Identification and localization of Nup170 in the microsporidian Nosema bombycis.Parasitology research · 2021Article
- Article
- Mapping the native organization of the yeast nuclear pore complex using nuclear radial intensity measurements.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Nuclear pore basket proteins are tethered to the nuclear envelope and can regulate membrane curvature.Developmental cell · 2015Article
- Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.Eukaryotic cell · 2009Review
- Global motions of the nuclear pore complex: insights from elastic network models.PLoS computational biology · 2009Article
- Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores.The Journal of cell biology · 2009Article
- The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly.The Journal of cell biology · 2009Article
- 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
- nup154 genetically interacts with cup and plays a cell-type-specific function during Drosophila melanogaster egg-chamber development.Genetics · 2007Article
- Nuclear pore complex function in Saccharomyces cerevisiae is influenced by glycosylation of the transmembrane nucleoporin Pom152p.Genetics · 2005Article
- Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates.The EMBO journal · 2005Article
- Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating.Molecular and cellular biology · 2003Article
- In situ analysis of spatial relationships between proteins of the nuclear pore complex.Biophysical journal · 2002Article
- Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly.BMC genetics · 2002Article
- The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex.The Journal of cell biology · 2001Article
- Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation.Genetics · 2001Article
- Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha.Molecular and cellular biology · 2000Article
- Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p.Molecular and cellular biology · 2000Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The FG nucleoporins are a conserved family of proteins, some of which bind to the nuclear localization sequence receptor, karyopherin. Distinct members of this family are found in each region of the nuclear pore complex (NPC), spanning from the cytoplasmically disposed filaments to the distal end of the nuclear basket. Movement of karyopherin from one FG nucleoporin to the next may be required for translocation of substrates across the NPC. So far, nothing is known about how the FG nucleoporins are localized within the NPC. To identify proteins that interact functionally with one member of this family, the Saccharomyces cerevisiae protein Nup1p, we previously identified 16 complementation groups containing mutants that are lethal in the absence of NUP1 These mutants were referred to as nle (Nup-lethal) mutants. Mutants in the nle3/nlel7 complementation group are lethal in combination with amino-terminal nup1 truncation mutants, which we have previously shown to be defective for localization to the NPC. Here we show that NLE3 (which is allelic to NUP170) encodes a protein with similarity to the mammalian nucleoporin Nup155. We show that Nle3p coprecipitates with glutathione S-transferase fusions containing the amino-terminal domain of Nup1p. Furthermore, a deletion of Nle3p leads to changes in the stoichiometry of several of the XFXFG nucleoporins, including the loss of Nup1p and Nup2p. These results suggest that Nle3p plays a role in localizing specific FG nucleoporins within the NPC. The broad spectrum of synthetic phenotypes observed with the nle3delta mutant provides support for this model. We also identify a redundant yeast homolog that can partially substitute for Nle3p and show that together these proteins are required for viability.
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