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Modulation of Nuclear Pore Topology by Transport Modifiers

Rainer D. Jäggi^*, Alfredo Franco-Obregón^*, Petra Mühlhäusser, Franziska Thomas, Ulrike Kutay and Klaus Ensslin^*

^* Solid State Physics Laboratory, ETH Zürich, 8093 Zürich, Switzerland and Institute of Biochemistry, ETH Zürich, 8093 Zürich, Switzerland

Correspondence: Address reprint requests to Klaus Ensslin, E-mail: ensslin{at}phys.ethz.ch.

The nuclear pore complex (NPC) represents the only pathway for macromolecular communication between the nuclear and cytoplasmic compartments of the cell. Nucleocytoplasmic transport requires the interaction of transport receptors with phenylalanine–glycine (FG)-repeats that line the transport pathway through the NPC. Here we examine the effects of transport receptors and amphipathic alcohols on NPC topology using scanning force microscopy. We show that transport receptors that irreversibly bind FG-repeats increase NPC vertical aspect, whereas transport receptors that weakly interact with FG-repeats increase NPC diameter. Interestingly, small polar alcohols likewise increase NPC diameter. These opposing effects agree with the inhibition or enhancement of nuclear transport, respectively, previously ascribed to these agents.

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				R. D. Jaggi, A. Franco-Obregon, and K. Ensslin Quantitative Topographical Analysis of Nuclear Pore Complex Function Using Scanning Force Microscopy Biophys. J., December 1, 2003; 85(6): 4093 - 4098. [Abstract] [Full Text] [PDF]