Cohesiveness tunes assembly and morphology of FG nucleoporin domain meshworks - Implications for nuclear pore permeability.
Nuclear pore complexes control the exchange of macromols. between the cytoplasm and the nucleus. A selective permeability barrier that arises from a supramol. assembly of intrinsically unfolded nucleoporin domains rich in phenylalanine-glycine dipeptides (FG domains) fills the nuclear pore. There is increasing evidence that selective transport requires cohesive FG domain interactions. To understand the functional roles of cohesive interactions, we studied monolayers of end-grafted FG domains as a bottom-up nanoscale model system of the permeability barrier. Based on detailed physicochem. anal. of the model films and comparison of the data with polymer theory, we propose that cohesiveness is tuned to promote rapid assembly of the permeability barrier and to generate a stable and compact pore-filling meshwork with a small mesh size. Our results highlight the functional importance of weak interactions, typically a few kBT per chain, and contribute important information to understand the mechanism of size-selective transport. [on SciFinder(R)]
Références
- Titre
- Cohesiveness tunes assembly and morphology of FG nucleoporin domain meshworks - Implications for nuclear pore permeability.
- Type de publication
- Article de revue
- Année de publication
- 2013
- Auteurs
- Eisele, Nico B., Labokha Aksana A., Frey Steffen, Gorlich Dirk, and Richter Ralf P.
- Revue
- Biophys. J.
- Volume
- 105
- Pagination
- 1860–1870
- ISSN
- 0006-3495
Soumis le 12 avril 2018