title: Lighting up the nuclear pore complex.
abstract: It is generally accepted that transport through the nuclear pore complex (NPC) involves an abundance of phenylalanine-glycine rich protein domains (FG-domains) that serve as docking sites for soluble nuclear transport receptors (NTRs) and their cargo complexes. But the precise mechanism of translocation through the NPC allowing for high speed and selectivity is still vividly debated. To ultimately decipher the underlying gating mechanism it is indispensable to shed more light on the molecular arrangement of FG-domains and the distribution of NTR-binding sites within the central channel of the NPC. In this review we revisit current transport models, summarize recent results regarding translocation through the NPC obtained by super-resolution microscopy and finally discuss the status and potential of optical methods in the analysis of the NPC.
authors.affiliation: Institute of Medical Physics and Biophysics, and Center for Nanotechnology (CeNTech), University of Muenster, Heisenbergstrasse 11, 48149 Muenster, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Kahms
authors.forename: Jana
authors.initials: J
authors.lastname: Hüve
authors.forename: Ramona
authors.initials: R
authors.lastname: Wesselmann
authors.forename: Julia C
authors.initials: JC
authors.lastname: Farr
authors.forename: Viola
authors.initials: V
authors.lastname: Baumgärtel
authors.forename: Reiner
authors.initials: R
authors.lastname: Peters
mesh_terms: D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D028861:Nuclear Pore Complex Proteins