title: Nanomechanical basis of selective gating by the nuclear pore complex.
abstract: The nuclear pore complex regulates cargo transport between the cytoplasm and the nucleus. We set out to correlate the governing biochemical interactions to the nanoscopic responses of the phenylalanineglycine (FG)-rich nucleoporin domains, which are involved in attenuating or promoting cargo translocation. We found that binding interactions with the transport receptor karyopherin-beta1 caused the FG domains of the human nucleoporin Nup153 to collapse into compact molecular conformations. This effect was reversed by the action of Ran guanosine triphosphate, which returned the FG domains into a polymer brush-like, entropic barrier conformation. Similar effects were observed in Xenopus oocyte nuclei in situ. Thus, the reversible collapse of the FG domains may play an important role in regulating nucleocytoplasmic transport.
authors.affiliation: M. E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland. roderick.lim@unibas.ch
authors.forename: Roderick Y H
authors.initials: RY
authors.lastname: Lim
authors.forename: Birthe
authors.initials: B
authors.lastname: Fahrenkrog
authors.forename: Joachim
authors.initials: J
authors.lastname: Köser
authors.forename: Kyrill
authors.initials: K
authors.lastname: Schwarz-Herion
authors.forename: Jie
authors.initials: J
authors.lastname: Deng
authors.forename: Ueli
authors.initials: U
authors.lastname: Aebi
mesh_terms: D021581:Active Transport, Cell Nucleus; D020816:Amino Acid Motifs; D000818:Animals; D005998:Glycine / Q000737:chemistry; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D016253:Microscopy, Immunoelectron; D022022:Nuclear Pore / Q000737:chemistry / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D010649:Phenylalanine / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D014982:Xenopus laevis; D028961:beta Karyopherins / Q000378:metabolism*; D020931:ran GTP-Binding Protein / Q000378:metabolism
chemical_list: C424166:KPNB1 protein, human; C079377:NUP153 protein, human; D028861:Nuclear Pore Complex Proteins; D028961:beta Karyopherins; D006153:Guanosine Diphosphate; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D020931:ran GTP-Binding Protein; D005998:Glycine