Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors
Summary - Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
March 27, 2018
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| In: |
Cell reports
Year: 2018, Jahrgang: 22, Heft: 13, Pages: 3660-3671 |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2018.03.022 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.1016/j.celrep.2018.03.022 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S2211124718303516 
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| Verfasserangaben: | Piau Siong Tan, Iker Valle Aramburu, Davide Mercadante, Swati Tyagi, Aritra Chowdhury, Daniel Spitz, Sarah L. Shammas, Frauke Gräter, Edward A. Lemke |
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| 245 | 1 | 0 | |a Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors |c Piau Siong Tan, Iker Valle Aramburu, Davide Mercadante, Swati Tyagi, Aritra Chowdhury, Daniel Spitz, Sarah L. Shammas, Frauke Gräter, Edward A. Lemke |
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| 520 | |a Summary - Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lower than in the archetypal-fuzzy complex between FG-Nup153 and NTRs. Unexpectedly, this behavior appears not to be encoded selectively into CRM1 but rather into the FG-Nup214 sequence. The same distinct binding mechanisms are unperturbed in O-linked β-N-acetylglucosamine-modified FG-Nups. Our results have implications for differential roles of distinctly spatially distributed FG-Nup⋅NTR interactions in the cell. | ||
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