Impact of distinct FG nucleoporin repeats on Nup98 self-association.

ABSTRACT: Nucleoporins rich in phenylalanine/glycine (FG) residues form the permeability barrier within the nuclear pore complex and are implicated in several pathological cellular processes, including oncogenic fusion condensates. The self-association of FG-repeat proteins and interactions between FG-repeats play a critical role in these activities by forming hydrogel-like structures. Here we show that mutation of specific FG repeats of Nup98 can strongly decrease the protein's self-association capabilities. We further present a cryo-electron microscopy structure of a Nup98 peptide fibril with higher stability per residue compared with previous Nup98 fibril structures. The high-resolution structure reveals zipper-like hydrophobic patches which contain a GLFG motif and are less compatible for bindin

SUBMITTER: Ibanez de Opakua A 

PROVIDER: S-EPMC11076500 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature