Minimal nuclear pore complexes define FG repeat domains essential for transport.

Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR
Nat Cell Biol. 2004 6 (3): 197-206

PMID: 15039779 · DOI:10.1038/ncb1097

Translocation through nuclear pore complexes (NPCs) requires interactions between receptor-cargo complexes and phenylalanine-glycine (FG) repeats in multiple FG domain-containing NPC proteins (FG-Nups). We have systematically deleted the FG domains of 11 Saccharomyces cerevisiae FG-Nups in various combinations. All five asymmetrically localized FG domains deleted together were non-essential. However, specific combinations of symmetrically localized FG domains were essential. Over half the total mass of FG domains could be deleted without loss of viability or the NPC's normal permeability barrier. Significantly, symmetric deletions caused mild reductions in Kap95-Kap60-mediated import rates, but virtually abolished Kap104 import. These results suggest the existence of multiple translocation pathways.

MeSH Terms (15)

Active Transport, Cell Nucleus beta Karyopherins Cell Membrane Permeability Cells, Cultured Cell Survival Gene Deletion Karyopherins Mutation Nuclear Pore Nuclear Pore Complex Proteins Protein Structure, Tertiary Protein Transport Repetitive Sequences, Amino Acid Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins

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