Modulation of nuclear pore topology by transport modifiers.
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.
Jäggi
Rainer D
RD
Solid State Physics Laboratory, ETH Zürich, Switzerland.
Franco-Obregón
Alfredo
A
Mühlhäusser
Petra
P
Thomas
Franziska
F
Kutay
Ulrike
U
Ensslin
Klaus
K
D021581:Active Transport, Cell Nucleus / Q000187:drug effects; D000438:Alcohols / Q000494:pharmacology; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism; D002478:Cells, Cultured; D018625:Microscopy, Atomic Force / Q000379:methods*; D022022:Nuclear Pore / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure*; D009865:Oocytes / Q000187:drug effects / Q000378:metabolism; D013501:Surface-Active Agents; D014981:Xenopus; D028961:beta Karyopherins / Q000235:genetics / Q000494:pharmacology
D000438:Alcohols; D000596:Amino Acids; D013501:Surface-Active Agents; D028961:beta Karyopherins