Chapter 3. Aspects of Nuclear Envelope Dynamics in Mitotic Cells
- Derek J. Chadwick Organizer,
- Jamie Goode
Published Online: 7 OCT 2008
DOI: 10.1002/0470093765.ch3
Copyright © Novartis Foundation 2005
Book Title
Nuclear Organization in Development and Disease: Novartis Foundation Symposium 264
Additional Information
How to Cite
Burke, B., Shanahan, C., Salina, D. and Crisp, M. (2008) Aspects of Nuclear Envelope Dynamics in Mitotic Cells, in Nuclear Organization in Development and Disease: Novartis Foundation Symposium 264 (eds D. J. Chadwick and J. Goode), John Wiley & Sons, Ltd, Chichester, UK. doi: 10.1002/0470093765.ch3
Publication History
- Published Online: 7 OCT 2008
- Published Print: 14 JAN 2005
ISBN Information
Print ISBN: 9780470093733
Online ISBN: 9780470093764
- Summary
- Chapter
Keywords:
- nuclear envelope (NE);
- inner and outer nuclear membranes (INM, ONM);
- INM localization;
- nuclear pore complexes (NPCs);
- cytoplasmic dynein;
- nuclear membrane dispersal;
- NPC proteins and mitotic function;
- Nup358;
- Nup358 SUMO ligase activity
Summary
Major features of the nuclear envelope (NE) are a pair of inner and outer nuclear membranes (INM, ONM) spanned by nuclear pore complexes. While the composition of the ONM resembles that of the endoplasmic reticulum, the INM contains a unique spectrum of proteins. Localization of INM proteins involves a mechanism of selective retention whereby integral proteins are immobilized and concentrated by virtue of interactions with nuclear components. In the case of emerin, INM localization involves interaction with A-type lamins. Interactions between membrane proteins may also play a significant role in INM localization. This conclusion stems from studies on nesprins, a family of membrane proteins that feature a large cytoplasmic domain, a single Cterminal membrane-spanning domain and a small lumenal domain. The nesprin membrane anchor and lumenal (KASH) domains are related to the Drosophila Klarsicht protein. Evidence is emerging that this KASH region interacts with other NE proteins and may influence their distributions. Overexpression of GFP-KASH causes loss of emerin and LAP2 from the NE. This is not due to global reorganization of the NE since LAP1 as well as lamins and NPCs remain unaffected. Our results suggest that interactions between NE membrane components are far more extensive and complex than current models suggest.