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MBC in Press, published online ahead of print April 20, 2005
Mol. Biol. Cell 10.1091/mbc.E04-11-1009

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Submitted on November 17, 2004
Revised on April 1, 2005
Accepted on April 12, 2005

Lamin A/C Dependent Localization of Nesprin-2, a Giant Scaffolder at the Nuclear Envelope

Thorsten Libotte,* Hafida Zaim,* Sabu Abraham,*{dagger} V. C. Padmakumar,*{dagger} Maria Schneider,* Wenshu Lu,* Martina Munck,* Christopher Hutchison,{ddagger} Manfred Wehnert,{sect} Birthe Fahrenkrog,|| Ursula Sauder,|| Ueli Aebi,|| Angelika A. Noegel,*{dagger} and Iakowos Karakesisoglou*

Centers for *Biochemistry and {dagger}Molecular Medicine Cologne, Medical Faculty, University of Cologne, 50931 Cologne, Germany; {sect}Institute of Human Genetics, Ernst-Moritz-Arndt-University, 17487 Greifswald, Germany; {ddagger}School of Biological and Biomedical Sciences, University of Durham, Durham, DH1 3LE United Kingdom; ||M. E. Mueller Institute, Biozentrum, University of Basel, CH-4056 Basel, Switzerland

Monitoring Editor: Orna Cohen-Fix

The vertebrate proteins Nesprin-1 and Nesprin-2 (also referred as Enaptin and NUANCE) together with ANC-1 of C. elegans and MSP-300 of D. melanogaster belong to a novel family of {alpha}-actinin type actin binding proteins residing at the nuclear membrane. Using biochemical techniques, we demonstrate that Nesprin-2 binds directly to emerin and the C-terminal common region of lamin A/C. Selective disruption of the lamin A/C network in COS7 cells using a dominant negative lamin B mutant, resulted in the redistribution of Nesprin-2. Furthermore, using lamin A/C knockout fibroblasts we show that lamin A/C is necessary for the nuclear envelope localization of Nesprin-2. In normal skin where lamin A/C is differentially expressed, strong Nesprin-2 expression was found in all epidermal layers, including the basal layer where only lamin C is present. This indicates that lamin C is sufficient for proper Nesprin-2 localization at the nuclear envelope. Expression of dominant negative Nesprin-2 constructs and knockdown studies in COS7 cells revealed that the presence of Nesprin-2 at the nuclear envelope is necessary for the proper localization of emerin. Our data imply a scaffolding function of Nesprin-2 at the nuclear membrane and suggest a potential involvement of this multi-isomeric protein in human disease.

Address correspondence to: Angelika A. Noegel (noegel{at}uni-koeln.de)




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