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2017 ; 8
(4
): 404-420
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Visualization of PML nuclear import complexes reveals FG-repeat nucleoporins at
cargo retrieval sites
#MMPMID28402725
Lång A
; Eriksson J
; Schink KO
; Lång E
; Blicher P
; Po?e? A
; Brech A
; Dalhus B
; Bøe SO
Nucleus
2017[Jul]; 8
(4
): 404-420
PMID28402725
show ga
Selective nuclear import in eukaryotic cells involves sequential interactions
between nuclear import receptors and phenylalanine-glycine (FG)-repeat
nucleoporins. Traditionally, binding of cargoes to import receptors is perceived
as a nuclear pore complex independent event, while interactions between import
complexes and nucleoporins are thought to take place at the nuclear pores.
However, studies have shown that nucleoporins are mobile and not static within
the nuclear pores, suggesting that they may become engaged in nuclear import
before nuclear pore entry. Here we have studied post-mitotic nuclear import of
the tumor suppressor protein PML. Since this protein forms nuclear compartments
called PML bodies that persist during mitosis, the assembly of putative PML
import complexes can be visualized on the surface of these protein aggregates as
the cell progress from an import inactive state in mitosis to an import active
state in G1. We show that these post-mitotic cytoplasmic PML bodies incorporate a
multitude of peripheral nucleoporins, but not scaffold or nuclear basket
nucleoporins, in a manner that depends on FG-repeats, the KPNB1 import receptor,
and the PML nuclear localization signal. The study suggests that nucleoporins
have the ability to target certain nuclear cargo proteins in a nuclear
pore-uncoupled state, before nuclear pore entry.