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First published online August 3, 2005
doi: 10.1242/10.1242/jcs.02471
Research Article |
1 Center for Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany
2 Center for Molecular Medicine Cologne, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany
3 Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, Department of Medical Biochemistry, Medical University of Vienna, Waehringer Guertel 18-20, A-1090 Vienna, Austria
* Authors for correspondence (e-mail: iakowos.karakesisoglou{at}uni-koeln.de; josef.gotzmann{at}meduniwien.ac.at)
Accepted 6 May 2005
Nesprins form a novel class of nuclear envelope-anchored spectrin-repeat proteins. We show that a direct association of their highly conserved C-terminal luminal domain with the inner nuclear membrane protein Sun1 mediates their nuclear envelope localisation. In Nesprin-1 and Nesprin-2 the conserved C-terminal amino acids PPPX are essential for the interaction with a C-terminal region in Sun1. In fact, Sun1 is required for the proper nuclear envelope localisation of Nesprin-2 as shown using dominant-negative mutants and by knockdown of Sun1 expression. Sun1 itself does not require functional A-type lamins for its localisation at the inner nuclear membrane in mammalian cells. Our findings propose a conserved nuclear anchorage mechanism between Caenorhabditis elegans and mammals and suggest a model in which Sun1 serves as a `structural bridge' connecting the nuclear interior with the actin cytoskeleton.
Key words: Emerin, Enaptin, Lamin A/C, NUANCE, SUN domain, Syne
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