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  Caspases target only two architectural components within the core structure of the nuclear pore complex.

Patre, M., Tabbert, A., Hermann, D., Walczak, H., Rackwitz, H. R., Cordes, V. C., et al. (2006). Caspases target only two architectural components within the core structure of the nuclear pore complex. Journal of Biological Chemistry, 281, 1296-1304. doi:10.1074/jbc.M511717200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3A8A-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3A8B-7
Genre: Journal Article

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Patre, M., Author
Tabbert, A., Author
Hermann, D., Author
Walczak, H., Author
Rackwitz, H. R., Author
Cordes, V. C.1, Author              
Ferrando-May, E., Author
Affiliations:
1Research Group of Nuclear Architecture, MPI for biophysical chemistry, Max Planck Society, ou_578575              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2005-11-142006-01-13
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.M511717200
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 281 Sequence Number: - Start / End Page: 1296 - 1304 Identifier: -