Multifunctionality of F-rich nucleoporins

Biochem Soc Trans. 2020 Dec 18;48(6):2603-2614. doi: 10.1042/BST20200357.

Abstract

Nucleoporins (Nups) represent a range of proteins most known for composing the macromolecular assembly of the nuclear pore complex (NPC). Among them, the family of intrinsically disordered proteins (IDPs) phenylalanine-glycine (FG) rich Nups, form the permeability barrier and coordinate the high-speed nucleocytoplasmic transport in a selective way. Those FG-Nups have been demonstrated to participate in various biological processes besides nucleocytoplasmic transport. The high number of accessible hydrophobic motifs of FG-Nups potentially gives rise to this multifunctionality, enabling them to form unique microenvironments. In this review, we discuss the multifunctionality of disordered and F-rich Nups and the diversity of their localizations, emphasizing the important roles of those Nups in various regulatory and metabolic processes.

Keywords: biological networks; gene expression and regulation; intrinsically disordered proteins; multifunctional proteins; nucleoporins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Active Transport, Cell Nucleus*
  • Amino Acid Motifs
  • Animals
  • Cell Lineage
  • Cell Nucleus / metabolism
  • Cilia / metabolism
  • Cytoplasm / metabolism
  • DNA Repair
  • Gene Expression Regulation
  • Glycine / metabolism*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Intrinsically Disordered Proteins / chemistry*
  • Neurodegenerative Diseases / metabolism
  • Nuclear Pore / metabolism*
  • Nuclear Pore Complex Proteins / metabolism*
  • Phenylalanine / chemistry*
  • Phenylalanine / metabolism
  • Protein Folding
  • Protein Transport

Substances

  • Intrinsically Disordered Proteins
  • Nuclear Pore Complex Proteins
  • Phenylalanine
  • Glycine