Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex.
Cell
; 171(4): 904-917.e19, 2017 Nov 02.
Article
em En
| MEDLINE
| ID: mdl-29033133
ABSTRACT
Nuclear pore complexes (NPCs) are â¼100 MDa transport channels assembled from multiple copies of â¼30 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.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
Poro Nuclear
Idioma:
En
Revista:
Cell
Ano de publicação:
2017
Tipo de documento:
Article