ArticleThe Journal of cell biology2011
Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Exportin-inspired artificial cell nuclear-exporting nanosystems.Nanoscale advances · 2022Article
- Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae.The Journal of cell biology · 2015Article
- An assay for clogging the ciliary pore complex distinguishes mechanisms of cytosolic and membrane protein entry.Current biology : CB · 2014Article
- High-resolution imaging reveals new features of nuclear export of mRNA through the nuclear pore complexes.International journal of molecular sciences · 2014Review
- Nuclear routing networks span between nuclear pore complexes and genomic DNA to guide nucleoplasmic trafficking of biomolecules.Journal of fertilization in vitro · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unraveling the organization of the FG repeat meshwork that forms the active transport channel of the nuclear pore complex (NPC) is key to understanding the mechanism of nucleocytoplasmic transport. In this paper, we develop a tool to probe the FG repeat network in living cells by modifying FG nucleoporins (Nups) with a binding motif (engineered dynein light chain-interacting domain) that can drag several copies of an interfering protein, Dyn2, into the FG network to plug the pore and stop nucleocytoplasmic transport. Our method allows us to specifically probe FG Nups in vivo, which provides insight into the organization and function of the NPC transport channel.
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Registered trials
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