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J. Biol. Chem., Vol. 281, Issue 2, 1296-1304, January 13, 2006

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Caspases Target Only Two Architectural Components within the Core Structure of the Nuclear Pore Complex^*

Monika Patre, Anja Tabbert, Daniela Hermann, Henning Walczak, Hans-Richard Rackwitz¶, Volker C. Cordes||**, and Elisa Ferrando-May1

From the Molecular Toxicology Group, Faculty of Biology, University of Konstanz, D-78457 Konstanz, Germany, the Tumor Immunology Program Division of Apoptosis Regulation, German Cancer Research Center, INF 280, D-69120 Heidelberg, Germany, the ^¶Peptide Specialty Laboratories GmbH, Sitzbuchweg 12, D-69118 Heidelberg, Germany, the ^||Department of Cell and Molecular Biology, Karolinska Institutet, S-17177 Stockholm, Sweden, and the ^**Zentrum fuer Molekulare Biologie Heidelberg, University of Heidelberg, INF 282, D-69120 Heidelberg, Germany

Caspases were recently implicated in the functional impairment of the nuclear pore complex during apoptosis, affecting its dual activity as nucleocytoplasmic transport channel and permeability barrier. Concurrently, electron microscopic data indicated that nuclear pore morphology is not overtly altered in apoptotic cells, raising the question of how caspases may deactivate nuclear pore function while leaving its overall structure largely intact. To clarify this issue we have analyzed the fate of all known nuclear pore proteins during apoptotic cell death. Our results show that only two of more than 20 nuclear pore core structure components, namely Nup93 and Nup96, are caspase targets. Both proteins are cleaved near their N terminus, disrupting the domains required for interaction with other nucleoporins actively involved in transport and providing the permeability barrier but dispensable for maintaining the nuclear pore scaffold. Caspase-mediated proteolysis of only few nuclear pore complex components may exemplify a general strategy of apoptotic cells to efficiently disable huge macromolecular machines.

Received for publication, October 31, 2005 , and in revised form, November 14, 2005.

^* This work was supported by grants from the Swedish Natural Research Council (to V. C. C.) and Deutsche Forschungsgemeinschaft Grant FOR 324/2-2 (to E. F.-M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1 and supplemental Table S2.

¹ To whom correspondence should be addressed: University of Konstanz, P.O. Box X911,D-78457 Konstanz, Germany. Tel.: 49-7531-884054; Fax: 49-7531-884033; E-mail: elisa.may{at}uni-konstanz.de.

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