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- Title
Interaction of nucleoporins with nuclear transport receptors: a structural perspective.
- Authors
Kehlenbach, Ralph H.; Neumann, Piotr; Ficner, Ralf; Dickmanns, Achim
- Abstract
Soluble nuclear transport receptors and stationary nucleoporins are at the heart of the nucleocytoplasmic transport machinery. A subset of nucleoporins contains characteristic and repetitive FG (phenylalanine-glycine) motifs, which are the basis for the permeability barrier of the nuclear pore complex (NPC) that controls transport of macromolecules between the nucleus and the cytoplasm. FG-motifs can interact with each other and/or with transport receptors, mediating their translocation across the NPC. The molecular details of homotypic and heterotypic FG-interactions have been analyzed at the structural level. In this review, we focus on the interactions of nucleoporins with nuclear transport receptors. Besides the conventional FG-motifs as interaction spots, a thorough structural analysis led us to identify additional similar motifs at the binding interface between nucleoporins and transport receptors. A detailed analysis of all known human nucleoporins revealed a large number of such phenylalanine-containing motifs that are not buried in the predicted 3D-structure of the respective protein but constitute part of the solvent-accessible surface area. Only nucleoporins that are rich in conventional FG-repeats are also enriched for these motifs. This additional layer of potential low-affinity binding sites on nucleoporins for transport receptors may have a strong impact on the interaction of transport complexes with the nuclear pore and, thus, the efficiency of nucleocytoplasmic transport.
- Subjects
NUCLEOPORINS; NUCLEAR transport; NUCLEOCYTOPLASMIC interactions; BINDING sites; SURFACE area
- Publication
Biological Chemistry, 2023, Vol 404, Issue 8/9, p791
- ISSN
1431-6730
- Publication type
Article
- DOI
10.1515/hsz-2023-0155