Visualization of PML nuclear import complexes reveals FG-repeat nucleoporins at cargo retrieval sites
| Autor: | Bjørn Dalhus, Anna Połeć, Andreas Brech, Pernille Blicher, Emma Lång, Stig Ove Bøe, Anna Lång, Jens Eriksson, Kay Oliver Schink |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Protein PML Phenylalanine Blotting Western Cell Cycle Active Transport Cell Nucleus Glycine Mitosis Cell Biology Biology Protein aggregation Virology Models Biological Cell biology Nuclear Pore Complex Proteins 03 medical and health sciences 030104 developmental biology Cytoplasm Nucleoporin Nuclear pore Nuclear transport Nuclear localization sequence Original Research |
| Zdroj: | Nucleus (Austin, Tex.). 8(4) |
| ISSN: | 1949-1042 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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