Minimal nuclear pore complexes define FG repeat domains essential for transport - PubMed (original) (raw)
doi: 10.1038/ncb1097. Epub 2004 Feb 22.
Affiliations
- PMID: 15039779
- DOI: 10.1038/ncb1097
Minimal nuclear pore complexes define FG repeat domains essential for transport
Lisa A Strawn et al. Nat Cell Biol. 2004 Mar.
Abstract
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.
Comment in
- Robbing from the pore.
Timney BL, Rout MP. Timney BL, et al. Nat Cell Biol. 2004 Mar;6(3):177-9. doi: 10.1038/ncb0304-177. Nat Cell Biol. 2004. PMID: 15039784 No abstract available.
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