Interaction of nucleoporins with nuclear transport receptors: a structural perspective
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.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Interaction of nucleoporins with nuclear transport receptors: a structural perspective ; volume:404 ; number:8-9 ; year:2023 ; pages:791-805 ; extent:015
Biological chemistry ; 404, Heft 8-9 (2023), 791-805 (gesamt 015)
- Urheber
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Kehlenbach, Ralph H.
Neumann, Piotr
Ficner, Ralf
Dickmanns, Achim
- DOI
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10.1515/hsz-2023-0155
- URN
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urn:nbn:de:101:1-2023090714134878434951
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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14.08.2025, 10:51 MESZ
Datenpartner
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Beteiligte
- Kehlenbach, Ralph H.
- Neumann, Piotr
- Ficner, Ralf
- Dickmanns, Achim
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