Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex
| Autor: | Leon Y. Chan, Pascal Vallotton, Annemarie Kralt, Carina Patrizia Derrer, Thomas U. Schwartz, Karsten Weis, Jeffrey H Tang, Evgeny Onischenko, Christopher F Mugler, Kevin E. Knockenhauer, Kasper R. Andersen |
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| Přispěvatelé: | Massachusetts Institute of Technology. Department of Biology, Andersen, Kasper R., Knockenhauer, Kevin Edward, Schwartz, Thomas |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Saccharomyces cerevisiae General Biochemistry Genetics and Molecular Biology Article Protein–protein interaction 03 medical and health sciences Journal Article otorhinolaryngologic diseases Nuclear pore Genetics Nuclear pore complex Nuclear pore biogenesis Nuclear pore structure Intrinsically disordered domains FG repeats Nuclear envelope Protein interactions Organelle Biogenesis biology biology.organism_classification Cell biology Nuclear Pore Complex Proteins stomatognathic diseases 030104 developmental biology Nuclear Pore Organelle biogenesis Nucleoporin Nuclear transport Biogenesis Function (biology) |
| Zdroj: | Cell, 171 (4) Onischenko, E, Tang, J H, Andersen, K R, Knockenhauer, K E, Vallotton, P, Derrer, C P, Kralt, A, Mugler, C F, Chan, L Y, Schwartz, T U & Weis, K 2017, ' Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex ', Cell, vol. 171, no. 4, pp. 904-917 . https://doi.org/10.1016/j.cell.2017.09.033 PMC |
| DOI: | 10.1016/j.cell.2017.09.033 |
| Popis: | 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 National Institutes of Health (U.S.) (Grant R01GM077537) |
| Databáze: | OpenAIRE |
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