We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
RanGTP mediates nuclear pore complex assembly.
- Authors
Walther, Tobias C.; Askjaer, Peter; Gentzel, Marc; Habermann, Anja; Griffiths, Gareth; Wilm, Matthias; Mattaj, Iain W.; Hetzer, Martin
- Abstract
In metazoa, the nuclear envelope breaks down and reforms during each cell cycle. Nuclear pore complexes (NPCs), which serve as channels for transport between the nucleus and cytoplasm(1), assemble into the reforming nuclear envelope in a sequential process involving association of a subset of NPC proteins, nucleoporins, with chromatin followed by the formation of a closed nuclear envelope fenestrated by NPCs[SUP2-7]. How chromatin recruitment of nucleoporins and NPC assembly are regulated is unknown. Here we demonstrate that RanGTP production is required to dissociate nucleoporins Nup107, Nup153 and Nup358 from Importin β, to target them to chromatin and to induce association between separate NPC subcom-plexes. Additionally, either an excess of RanGTP or removal of Importin β induces formation of NPC-containing membrane structures-annulate lamellae-both in vitro in the absence of chromatin and in vivo. Annulate lamellae formation is strongly and specifically inhibited by an excess of Importin β. The data demonstrate that RanGTP triggers distinct steps of NPC assembly, and suggest a mechanism for the spatial restriction of NPC assembly to the surface of chromatin.
- Subjects
CELL nuclei; CELL cycle; GUANOSINE triphosphate; CHROMATIN
- Publication
Nature, 2003, Vol 424, Issue 6949, p689
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/nature01898