Floppy but not sloppy: interaction mechanism of FG-nucleoporins and nuclear transport receptors
The nuclear pore complex (NPC) forms a permeability barrier between the nucleus and the cytoplasm. Molecules that are able to cross this permeability barrier encounter different disordered phenylalanine glycine rich nucleoporins (FG-Nups) that act as a molecular filter and regulate the selective NPC...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
30 June 2017
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| In: |
Seminars in cell & developmental biology
Year: 2017, Jahrgang: 68, Pages: 34-41 |
| ISSN: | 1096-3634 |
| DOI: | 10.1016/j.semcdb.2017.06.026 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1016/j.semcdb.2017.06.026 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S108495211730294X 
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| Verfasserangaben: | Iker Valle Aramburu, Edward A. Lemke |
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| 520 | |a The nuclear pore complex (NPC) forms a permeability barrier between the nucleus and the cytoplasm. Molecules that are able to cross this permeability barrier encounter different disordered phenylalanine glycine rich nucleoporins (FG-Nups) that act as a molecular filter and regulate the selective NPC crossing of biomolecules. In this review, we provide a current overview regarding the interaction mechanism between FG-Nups and the carrier molecules that recognize and enable the transport of cargoes through the NPC aiming to understand the general molecular mechanisms that facilitate the nucleocytoplasmic transport. | ||
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