Amyloids are fibrillar protein aggregates with a cross-β structure and unusual features, including high resistance to detergent or protease treatment. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Several examples of nucleoporins (e.g., yeast Nup49, Nup100, Nup116, and human NUP153) are supposed to form amyloid fibrils. In this study, we demonstrated an ability of the human NUP58 nucleoporin to form amyloid aggregates in vivo and in vitro. Moreover, we found two forms of NUP58 aggregates: oligomers and polymers stabilized by disulfide bonds. Bioinformatic analysis revealed that all known orthologs of this protein are potential amyloids which possess several regions with conserved ability to aggregation. The biological role of nucleoporin amyloid formation is debatable. We suggest that it is a rather abnormal process, which is characteristic for many proteins implicated in phase separation.
Original languageEnglish
Article number1451
Number of pages12
JournalBiomedicines
Volume9
Issue number10
DOIs
StatePublished - 13 Oct 2021

    Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine (miscellaneous)

    Research areas

  • ArchCandy, C-DAG, Congo Red, Evolution, Human amyloids, Nucleoporins, Protein aggregation, human amyloids, BARRIER, PRION, evolution, nucleoporins, PREDICTION, protein aggregation, PROTEINS, AGGREGATION, NUCLEAR-PORES, PLASTICITY

ID: 86420176