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Abstract
Exchange of macromolecules between the cytoplasm and the nucleus of all eukaryotic cells is controlled by nuclear pore complexes, which form a selective permeability barrier. The requirement for rapid but selective transport leads to a "transport paradox." A new experimental study now provides a thermodynamic explanation.
Highlights
Vital functions such as gene expression, cell growth, and cell division critically depend on the continuous passage of molecules from the nucleus to the cytoplasm and vice versa
In this exciting Accelerated Communication, Cowburn and co-workers (2) provide a possible explanation by carefully examining the energetics of multivalent interactions using a combination of calorimetry and NMR spectroscopy
The authors show that individual FSFG-mediated interactions are of low affinity and that multiplexing the number of interaction sites does not lead to a synergistic increase in affinity
Summary
Vital functions such as gene expression, cell growth, and cell division critically depend on the continuous passage of molecules from the nucleus to the cytoplasm and vice versa. 2 The abbreviations used are: NPC, nuclear pore complex; IDP, intrinsically disordered protein; TF, transport factor; FG Nup, Phe–Gly nucleoporin. Nuclear transport factor 2 (NTF2) and constructs with variable numbers of FSFG motifs.
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