Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors.

Abstract : The mechanisms by which intrinsically disordered proteins engage in rapid and highly selective binding is a subject of considerable interest and represents a central paradigm to nuclear pore complex (NPC) function, where nuclear transport receptors (NTRs) move through the NPC by binding disordered phenylalanine-glycine-rich nucleoporins (FG-Nups). Combining single-molecule fluorescence, molecular simulations, and nuclear magnetic resonance, we show that a rapidly fluctuating FG-Nup populates an ensemble of conformations that are prone to bind NTRs with near diffusion-limited on rates, as shown by stopped-flow kinetic measurements. This is achieved using multiple, minimalistic, low-affinity binding motifs that are in rapid exchange when engaging with the NTR, allowing the FG-Nup to maintain an unexpectedly high plasticity in its bound state. We propose that these exceptional physical characteristics enable a rapid and specific transport mechanism in the physiological context, a notion supported by single molecule in-cell assays on intact NPCs.
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Article dans une revue
Cell, Elsevier, 2015, 163 (3), pp.734-45
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Soumis le : lundi 30 novembre 2015 - 10:08:11
Dernière modification le : lundi 11 février 2019 - 16:50:30

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Sigrid Milles, Davide Mercadante, Iker Valle Aramburu, Malene Ringkjøbing Jensen, Niccolò Banterle, et al.. Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors.. Cell, Elsevier, 2015, 163 (3), pp.734-45. 〈hal-01235362〉



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