Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex
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Author(s)
Onischenko, Evgeny
Tang, Jeffrey H.
Vallotton, Pascal
Derrer, Carina P.
Kralt, Annemarie
Mugler, Christopher F.
Chan, Leon Y.
Weis, Karsten
Andersen, Kasper R.
Knockenhauer, Kevin Edward
Date Issued
October 2017
Journal
Cell
Publisher
Elsevier BV
Citation
Onischenko, Evgeny et al. “Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex.” Cell 171, 4 (November 2017): 904–917 © 2017 Elsevier Inc
Version
Author's final manuscript
Abstract
Nuclear pore complexes (NPCs) are ∼100 MDa transport channels assembled from multiple copies of ∼30 nucleoporins (Nups). One-third of these Nups contain phenylalanine-glycine (FG)-rich repeats, forming a diffusion barrier, which is selectively permeable for nuclear transport receptors that interact with these repeats. Here, we identify an additional function of FG repeats in the structure and biogenesis of the yeast NPC. We demonstrate that GLFG-containing FG repeats directly bind to multiple scaffold Nups in vitro and act as NPC-targeting determinants in vivo. Furthermore, we show that the GLFG repeats of Nup116 function in a redundant manner with Nup188, a nonessential scaffold Nup, to stabilize critical interactions within the NPC scaffold needed for late steps of NPC assembly. Our results reveal a previously unanticipated structural role for natively unfolded GLFG repeats as Velcro to link NPC subcomplexes and thus add a new layer of connections to current models of the NPC architecture. In addition to forming the permeability barrier, FG repeats in nucleoporins contribute structurally to nuclear pore biogenesis and function. Keywords: Nuclear pore complex; Nuclear pore biogenesis; Nuclear pore structure; Intrinsically disordered domains; FG repeats; Nuclear envelope; Protein interactions
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/J.CELL.2017.09.033
