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Caspases Disrupt the Nuclear-Cytoplasmic Barrier
During apoptosis, caspases, a family of proteases, disassemble a cell by cleaving a set of proteins. Caspase-3 plays a major role in the disassembly of the nucleus by processing several nuclear substrates. The question is how caspase-3, which is usually cytoplasmic, gains access to its nuclear targe...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2000
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174353/ https://www.ncbi.nlm.nih.gov/pubmed/11085998 |
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author | Faleiro, Lavina Lazebnik, Yuri |
author_facet | Faleiro, Lavina Lazebnik, Yuri |
author_sort | Faleiro, Lavina |
collection | PubMed |
description | During apoptosis, caspases, a family of proteases, disassemble a cell by cleaving a set of proteins. Caspase-3 plays a major role in the disassembly of the nucleus by processing several nuclear substrates. The question is how caspase-3, which is usually cytoplasmic, gains access to its nuclear targets. It was suggested that caspase-3 is actively transported to the nucleus through the nuclear pores. We found that caspase-9, which is activated earlier than caspase-3, directly or indirectly inactivates nuclear transport and increases the diffusion limit of the nuclear pores. This increase allows caspase-3 and other molecules that could not pass through the nuclear pores in living cells to enter or leave the nucleus during apoptosis by diffusion. Hence, caspase-9 contributes to cell disassembly by disrupting the nuclear-cytoplasmic barrier. |
format | Text |
id | pubmed-2174353 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21743532008-05-01 Caspases Disrupt the Nuclear-Cytoplasmic Barrier Faleiro, Lavina Lazebnik, Yuri J Cell Biol Original Article During apoptosis, caspases, a family of proteases, disassemble a cell by cleaving a set of proteins. Caspase-3 plays a major role in the disassembly of the nucleus by processing several nuclear substrates. The question is how caspase-3, which is usually cytoplasmic, gains access to its nuclear targets. It was suggested that caspase-3 is actively transported to the nucleus through the nuclear pores. We found that caspase-9, which is activated earlier than caspase-3, directly or indirectly inactivates nuclear transport and increases the diffusion limit of the nuclear pores. This increase allows caspase-3 and other molecules that could not pass through the nuclear pores in living cells to enter or leave the nucleus during apoptosis by diffusion. Hence, caspase-9 contributes to cell disassembly by disrupting the nuclear-cytoplasmic barrier. The Rockefeller University Press 2000-11-27 /pmc/articles/PMC2174353/ /pubmed/11085998 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Original Article Faleiro, Lavina Lazebnik, Yuri Caspases Disrupt the Nuclear-Cytoplasmic Barrier |
title | Caspases Disrupt the Nuclear-Cytoplasmic Barrier |
title_full | Caspases Disrupt the Nuclear-Cytoplasmic Barrier |
title_fullStr | Caspases Disrupt the Nuclear-Cytoplasmic Barrier |
title_full_unstemmed | Caspases Disrupt the Nuclear-Cytoplasmic Barrier |
title_short | Caspases Disrupt the Nuclear-Cytoplasmic Barrier |
title_sort | caspases disrupt the nuclear-cytoplasmic barrier |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174353/ https://www.ncbi.nlm.nih.gov/pubmed/11085998 |
work_keys_str_mv | AT faleirolavina caspasesdisruptthenuclearcytoplasmicbarrier AT lazebnikyuri caspasesdisruptthenuclearcytoplasmicbarrier |