PT  - JOURNAL ARTICLE
AU  - George J Stanley
AU  - Ariberto Fassati
AU  - Bart W Hoogenboom
TI  - Atomic force microscopy reveals structural variability amongst nuclear pore complexes
AID  - 10.26508/lsa.201800142
DP  - 2018 Aug 01
TA  - Life Science Alliance
PG  - e201800142
VI  - 1
IP  - 4
4099  - https://www.life-science-alliance.org/content/1/4/e201800142.short
4100  - https://www.life-science-alliance.org/content/1/4/e201800142.full
SO  - Life Sci. Alliance2018 Aug 01; 1
AB  - The nuclear pore complex (NPC) is a proteinaceous assembly that regulates macromolecular transport into and out of the nucleus. Although the structure of its scaffold is being revealed in increasing detail, its transport functionality depends upon an assembly of intrinsically disordered proteins (called FG-Nups) anchored inside the pore's central channel, which have hitherto eluded structural characterization. Here, using high-resolution atomic force microscopy, we provide a structural and nanomechanical analysis of individual NPCs. Our data highlight the structural diversity and complexity at the nuclear envelope, showing the interplay between the lamina network, actin filaments, and the NPCs. It reveals the dynamic behaviour of NPC scaffolds and displays pores of varying sizes. Of functional importance, the NPC central channel shows large structural diversity, supporting the notion that FG-Nup cohesiveness is in a range that facilitates collective rearrangements at little energetic cost. Finally, different nuclear transport receptors are shown to interact in qualitatively different ways with the FG-Nups, with particularly strong binding of importin-β.