| Literature DB >> 28669824 |
Iker Valle Aramburu1, Edward A Lemke2.
Abstract
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.Entities:
Keywords: Intrinsically disordered protein; Multivalency; Nuclear transport receptors; Nucleocytoplasmic transport; Nucleoporins
Mesh:
Substances:
Year: 2017 PMID: 28669824 DOI: 10.1016/j.semcdb.2017.06.026
Source DB: PubMed Journal: Semin Cell Dev Biol ISSN: 1084-9521 Impact factor: 7.727