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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Bibliographic Details
Main Authors: Aramburu, Iker Valle (Author) , Lemke, Edward A. (Author)
Format: Article (Journal)
Language:English
Published: 30 June 2017
In: Seminars in cell & developmental biology
Year: 2017, Volume: 68, Pages: 34-41
ISSN:1096-3634
DOI:10.1016/j.semcdb.2017.06.026
Online Access: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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Author Notes:Iker Valle Aramburu, Edward A. Lemke
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Summary: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.
Item Description:Gesehen am 24.09.2018
Physical Description:Online Resource
ISSN:1096-3634
DOI:10.1016/j.semcdb.2017.06.026