Viruses, microorganisms and scientists meet the nuclear pore
Open Access
- 15 January 1999
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 18 (2) , 289-296
- https://doi.org/10.1093/emboj/18.2.289
Abstract
The modular architecture of the nuclear pore complex (NPC) consists of a membrane‐embedded basic framework (the ‘spoke complex’) made up of eight multidomain spokes with two rings on each face (Figure 1A). The ring facing the cytoplasm is decorated with eight ∼50 nm fibrils extending into the cytosol, and the nuclear ring is capped with a basket‐like assembly of eight thin, 50–100 nm filaments joined distally by a 30–40 nm diameter terminal ring. The center of the basic framework harbors the ‘gated transport channel’, which is involved in signal‐mediated bidirectional transport of macromolecules and is plugged to the central ‘transporter’, whose ultimate structure and functional role in mediated nuclear transport remains to be established. N.Panté and U.Aebi (Basel) reported their approaches to the functional roles of the different NPC components and to dissection of the steps of nuclear import and export at the NPC by direct visualization of gold‐labeled proteins and RNAs moving in or out of the cell nucleus through the NPC (Figure 1B). Figure 1. ( A ) Current consensus model of the membrane‐bound NPC. Its major structural components include the basic framework, the central plug or gated channel, the cytoplasmic and nuclear rings, and the cytoplasmic fibrils and nuclear basket. ( B ) Visualization of the different steps of nuclear import of an NLS‐bearing protein through the NPC. At the bottom are selected examples of cross‐sectioned NPCs with associated nucleoplasmin–gold particles (8 nm diameter), depicted at different stages of transport; at the top is a schematic diagram of the distinct steps visualized by electron microscopy. In the first step of transport, the NLS protein to be imported associates with the NLS receptor (importins α and β) (1). This step takes place in the cytoplasm and does not require physical interaction with any NPC component. In a second step, this ‘targeting complex’ docks …Keywords
This publication has 29 references indexed in Scilit:
- Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during InfectionPlant Cell, 1998
- Recognition of bacterial avirulence proteins occurs inside the plant cell: a general phenomenon in resistance to bacterial diseases?The Plant Journal, 1997
- Nuclear protein importCurrent Opinion in Cell Biology, 1997
- Importin α- from Arabidopsis thaliana Is a Nuclear Import Receptor That Recognizes Three Classes of Import SignalsPlant Physiology, 1997
- A plant in vitro system for the nuclear import of proteinsThe Plant Journal, 1996
- Getting it together in plant virus movement: cooperative interactions between bipartite geminivirus movement proteinsTrends in Cell Biology, 1996
- Actin-based motility of vaccinia virusNature, 1995
- HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integraseCell, 1995
- HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulatorCell, 1995
- Physical properties of cytoplasmCurrent Opinion in Cell Biology, 1994