| Literature DB >> 12524319 |
Rainer D Jäggi1, Alfredo Franco-Obregón, Petra Mühlhäusser, Franziska Thomas, Ulrike Kutay, Klaus Ensslin.
Abstract
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.Entities:
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Year: 2003 PMID: 12524319 PMCID: PMC1302647 DOI: 10.1016/S0006-3495(03)74886-3
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033