Lighting up the nuclear pore complex

Kahms M., Hüve J., Wesselmann R., Farr J., Baumgärtel V., Peters R.

Research article (journal) | Peer reviewed

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. © 2011 Elsevier GmbH.

Details about the publication

JournalEuropean Journal of Cell Biology
Volume90
Issue9
Page range751-758
StatusPublished
Release year2011
Language in which the publication is writtenEnglish
DOI10.1016/j.ejcb.2011.04.004
Link to the full texthttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79960557348∨igin=inward
KeywordsFG repeats; Nuclear pore complex; Nuclear transport; Nuclear transport receptor; Super-resolution microscopy; Transport model

Authors from the University of Münster

Hüve, Jana
Institute of Medical Physics and Biophysics
Kahms, Martin
Institute of Medical Physics and Biophysics