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Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells

Entry into mitosis in vertebrate cells is guarded by a checkpoint that can be activated by a variety of insults, including chromosomal damage and disrupting microtubules (Rieder, C.L., and R.W. Cole. 1998. J. Cell Biol. 142:1013–1022; Rieder, C.L., and R.W. Cole. 2000. Curr. Biol. 10:1067–1070). Thi...

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Autores principales: Matsusaka, Takahiro, Pines, Jonathon
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172205/
https://www.ncbi.nlm.nih.gov/pubmed/15302856
http://dx.doi.org/10.1083/jcb.200401139
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author Matsusaka, Takahiro
Pines, Jonathon
author_facet Matsusaka, Takahiro
Pines, Jonathon
author_sort Matsusaka, Takahiro
collection PubMed
description Entry into mitosis in vertebrate cells is guarded by a checkpoint that can be activated by a variety of insults, including chromosomal damage and disrupting microtubules (Rieder, C.L., and R.W. Cole. 1998. J. Cell Biol. 142:1013–1022; Rieder, C.L., and R.W. Cole. 2000. Curr. Biol. 10:1067–1070). This checkpoint acts at the end of interphase to delay cells from entering mitosis, causing cells in prophase to decondense their chromosomes and return to G2 phase. Here, we show that in response to microtubule poisons this “antephase” checkpoint is primarily mediated by the p38 stress kinases and requires the Chfr protein that is absent or inactive in several transformed cell lines (Scolnick, D.M., and T.D. Halazonetis. 2000. Nature. 406:430–435) and lung tumors (Mizuno, K., H. Osada, H. Konishi, Y. Tatematsu, Y. Yatabe, T. Mitsudomi, Y. Fujii, and T. Takahashi. 2002. Oncogene. 21:2328–2333). Furthermore, in contrast to previous reports, we find that the checkpoint requires ubiquitylation but not proteasome activity, which is in agreement with the recent demonstration that Chfr conjugates ubiquitin through lysine 63 and not lysine 48 (Bothos, J., M.K. Summers, M. Venere, D.M. Scolnick, and T.D. Halazonetis. 2003. Oncogene. 22:7101–7107).
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spelling pubmed-21722052008-03-05 Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells Matsusaka, Takahiro Pines, Jonathon J Cell Biol Research Articles Entry into mitosis in vertebrate cells is guarded by a checkpoint that can be activated by a variety of insults, including chromosomal damage and disrupting microtubules (Rieder, C.L., and R.W. Cole. 1998. J. Cell Biol. 142:1013–1022; Rieder, C.L., and R.W. Cole. 2000. Curr. Biol. 10:1067–1070). This checkpoint acts at the end of interphase to delay cells from entering mitosis, causing cells in prophase to decondense their chromosomes and return to G2 phase. Here, we show that in response to microtubule poisons this “antephase” checkpoint is primarily mediated by the p38 stress kinases and requires the Chfr protein that is absent or inactive in several transformed cell lines (Scolnick, D.M., and T.D. Halazonetis. 2000. Nature. 406:430–435) and lung tumors (Mizuno, K., H. Osada, H. Konishi, Y. Tatematsu, Y. Yatabe, T. Mitsudomi, Y. Fujii, and T. Takahashi. 2002. Oncogene. 21:2328–2333). Furthermore, in contrast to previous reports, we find that the checkpoint requires ubiquitylation but not proteasome activity, which is in agreement with the recent demonstration that Chfr conjugates ubiquitin through lysine 63 and not lysine 48 (Bothos, J., M.K. Summers, M. Venere, D.M. Scolnick, and T.D. Halazonetis. 2003. Oncogene. 22:7101–7107). The Rockefeller University Press 2004-08-16 /pmc/articles/PMC2172205/ /pubmed/15302856 http://dx.doi.org/10.1083/jcb.200401139 Text en Copyright © 2004, 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 Research Articles
Matsusaka, Takahiro
Pines, Jonathon
Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
title Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
title_full Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
title_fullStr Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
title_full_unstemmed Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
title_short Chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
title_sort chfr acts with the p38 stress kinases to block entry to mitosis in mammalian cells
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172205/
https://www.ncbi.nlm.nih.gov/pubmed/15302856
http://dx.doi.org/10.1083/jcb.200401139
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