ArticleBiophysical journal2002
In situ analysis of spatial relationships between proteins of the nuclear pore complex.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- FRET Microscopy in Yeast.Biosensors · 2019Review
- 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
- The nuclear pore complex: understanding its function through structural insight.Nature reviews. Molecular cell biology · 2017Review
- Article
- Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export.Molecular and cellular biology · 2008Article
- Combining guilt-by-association and guilt-by-profiling to predict Saccharomyces cerevisiae gene function.Genome biology · 2008Article
- The visible touch: in planta visualization of protein-protein interactions by fluorophore-based methods.Plant methods · 2006Article
- Retroviruses and yeast retrotransposons use overlapping sets of host genes.Genome research · 2005Article
- The two tempos of nuclear pore complex evolution: highly adapting proteins in an ancient frozen structure.Genome biology · 2005Article
- A fluorescence resonance energy transfer-derived structure of a quantum dot-protein bioconjugate nanoassembly.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex.Molecular biology of the cell · 2003Article
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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
Macromolecular transport between the nucleus and cytoplasm occurs through the nuclear pore complexes (NPCs). The NPC in the budding yeast Saccharomyces cerevisiae is a 60-MDa structure embedded in the nuclear envelope and composed of ~30 proteins, termed nucleoporins or nups. Here we present a large-scale analysis of spatial relationships between nucleoporins using fluorescence resonance energy transfer (FRET) in living yeast cells. Energy transfer was measured in a panel of strains, each of which coexpresses the enhanced cyan and yellow fluorescent proteins as fusions to distinct nucleoporins. With this approach, we have determined 13 nucleoporin pairs yielding FRET signals. Independent experiments are consistent with the FRET results: Nup120 localization is perturbed in the nic96-1 mutant, as is Nup82 localization in the nup116Delta mutant. To better understand the spatial relationship represented by an in vivo FRET signal, we have investigated the requirements of these signals. We demonstrate that in one case FRET signal is lost upon insertion of a short spacer between the nucleoporin and its enhanced yellow fluorescent protein label. We also show that the Nup120 FRET signals depend on whether the fluorescent moiety is fused to the N- or C-terminus of Nup120. Combined with existing data on NPC structure, the FRET pairs identified in this study allow us to propose a refined molecular model of the NPC. We suggest that the approach may serve as a prototype for the in situ study of other large macromolecular complexes.
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