ArticleProceedings of the National Academy of Sciences of the United States of America1999
Optical recording of signal-mediated protein transport through single nuclear pore complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Mapping the Direction of Nucleocytoplasmic Transport of Glucocorticoid Receptor (GR) in Live Cells Using Two-Foci Cross-Correlation in Massively Parallel Fluorescence Correlation Spectroscopy (mpFCS).Analytical chemistry · 2023Article
- The coming-of-age of nucleocytoplasmic transport in motor neuron disease and neurodegeneration.Cellular and molecular life sciences : CMLS · 2019Review
- Dissecting in vivo steady-state dynamics of karyopherin-dependent nuclear transport.Molecular biology of the cell · 2016Article
- Attolitre-sized lipid bilayer chamber array for rapid detection of single transporters.Scientific reports · 2015Article
- Nanoscale stiffness topography reveals structure and mechanics of the transport barrier in intact nuclear pore complexes.Nature nanotechnology · 2015Article
- Arrayed lipid bilayer chambers allow single-molecule analysis of membrane transporter activity.Nature communications · 2014Article
- Nanoscale mechanism of molecular transport through the nuclear pore complex as studied by scanning electrochemical microscopy.Journal of the American Chemical Society · 2013Article
- Multiscale dynamics in nucleocytoplasmic transport.Current opinion in cell biology · 2012Review
- Domain topology of nucleoporin Nup98 within the nuclear pore complex.Journal of structural biology · 2012Article
- Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex.Journal of cell science · 2010Article
- 4Pi microscopy of the nuclear pore complex.Biophysical journal · 2008Article
- Reversibility in nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo.The Journal of cell biology · 2006Article
- Optical microwell assay of membrane transport kinetics.Biophysical journal · 2003Article
- Reconstitution of nuclear protein export in isolated nuclear envelopes.The Journal of cell biology · 2002Article
- Both ran and importins have the ability to function as nuclear mRNA export factors.RNA (New York, N.Y.) · 2002Article
- Transport into and out of the nucleus.Microbiology and molecular biology reviews : MMBR · 2001Review
- Kinetics and mechanism of DNA uptake into the cell nucleus.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Kinetic analysis of translocation through nuclear pore complexes.The EMBO journal · 2001Article
- Kinetics of protein import into isolated Xenopus oocyte nuclei.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Optical single-transporter recording, a recently established fluorescence microscopic method, was used to study the selective transport of proteins through single nuclear pore complexes (NPCs) of Xenopus oocytes. Recombinant proteins containing either a nuclear localization signal (import protein) or a nuclear export signal (export protein) were generated as transport substrates. To approximate in vivo conditions as closely as possible, a Xenopus egg extract was applied to the cytosolic side and a Xenopus oocyte nuclear extract to the nuclear side of the NPCs. It was found that protein transport through functionally isolated, "patched" NPCs depended on signal sequences, extracts, and metabolic energy, as in vivo. All NPCs were competent for both import and export. The transport direction was strictly determined by the transport signal, and at none of the conditions explored was the import protein exported or the export protein imported, even when the application sides of the extracts were reversed. The mean transport rates of the single NPC were approximately 2 dimers/s for the import protein and approximately 4 dimers/s for the export protein ( approximately 15 microM substrate concentration, 22-24 degrees C), in good agreement with in vivo rates estimated for mammalian cells by microinjection experiments. The study shows that optical single-transporter recording permits the analysis of membrane transport processes not previously accessible to single-transporter recording and thus provides additional possibilities for the elucidation of nucleocytoplasmic transport mechanisms.
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