Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
Biophys J
2003 Dec 01;856:4093-8. doi: 10.1016/S0006-3495(03)74821-8.
Show Gene links
Show Anatomy links
Quantitative topographical analysis of nuclear pore complex function using scanning force microscopy.
Jäggi RD
,
Franco-Obregón A
,
Ensslin K
.
???displayArticle.abstract???
The only avenue for macromolecular communication between nucleoplasmic and cytoplasmic compartments of the cell is through the nuclear pore complexes (NPCs), which are thus situated at a key location for the control of downstream transcriptional processes. The translocation of cargo through the NPC is mediated by transport receptors, which have the difficult task of making specific, yet transitory, interactions with the NPC in order to support efficient transport. In this report we have examined two stages in the translocation process using scanning force microscopy. We show that the initial docking of importin beta 45-462 is rapid and occurs at nanomolar concentrations. Later stages of transport involve translocation through the central lumen of the NPC and are thought to involve hydrophobic interactions between transport receptors and the NPC. Using calcium-depleted nuclear envelopes we argue that luminal regions of the NPC exhibit hydrophobic characteristics that are not observed for other regions of the NPC.
Akey,
Visualization of transport-related configurations of the nuclear pore transporter.
1990, Pubmed
Akey,
Visualization of transport-related configurations of the nuclear pore transporter.
1990,
Pubmed
Akey,
Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy.
1993,
Pubmed
,
Xenbase
Akey,
Structural plasticity of the nuclear pore complex.
1995,
Pubmed
,
Xenbase
Bayliss,
Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking.
2000,
Pubmed
Bickel,
The nuclear pore complex mystery and anomalous diffusion in reversible gels.
2002,
Pubmed
Danker,
Nuclear pore function viewed with atomic force microscopy.
2000,
Pubmed
Görlich,
Transport between the cell nucleus and the cytoplasm.
1999,
Pubmed
Jäggi,
Modulation of nuclear pore topology by transport modifiers.
2003,
Pubmed
,
Xenbase
Kutay,
Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex.
1997,
Pubmed
,
Xenbase
Moore-Nichols,
Regulation of nuclear pore complex conformation by IP(3) receptor activation.
2002,
Pubmed
,
Xenbase
Müller,
Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope.
1999,
Pubmed
Panté,
Molecular dissection of the nuclear pore complex.
1996,
Pubmed
Perez-Terzic,
Conformational states of the nuclear pore complex induced by depletion of nuclear Ca2+ stores.
1996,
Pubmed
,
Xenbase
Radu,
The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex.
1995,
Pubmed
Ribbeck,
Kinetic analysis of translocation through nuclear pore complexes.
2001,
Pubmed
Ribbeck,
The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion.
2002,
Pubmed
Rout,
The yeast nuclear pore complex: composition, architecture, and transport mechanism.
2000,
Pubmed
Stewart,
Insights into the molecular mechanism of nuclear trafficking using nuclear transport factor 2 (NTF2).
2000,
Pubmed
Stoffler,
Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy.
1999,
Pubmed
,
Xenbase
Stoffler,
The nuclear pore complex: from molecular architecture to functional dynamics.
1999,
Pubmed
Walther,
The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import.
2002,
Pubmed
,
Xenbase
Wang,
Conformational changes of the in situ nuclear pore complex.
1999,
Pubmed
,
Xenbase
