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Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation
Eg5 (kinesin-5) is a highly conserved microtubule motor protein, essential for centrosome separation and bipolar spindle assembly in human cells. Using an “in vitro” evolution approach, we generated human cancer cells that can grow in the complete absence of Eg5 activity. Characterization of these E...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3656018/ https://www.ncbi.nlm.nih.gov/pubmed/23713137 http://dx.doi.org/10.4161/cib.23841 |
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author | van Heesbeen, Roy G.H.P. Raaijmakers, Jonne A. Tanenbaum, Marvin E. Medema, René H. |
author_facet | van Heesbeen, Roy G.H.P. Raaijmakers, Jonne A. Tanenbaum, Marvin E. Medema, René H. |
author_sort | van Heesbeen, Roy G.H.P. |
collection | PubMed |
description | Eg5 (kinesin-5) is a highly conserved microtubule motor protein, essential for centrosome separation and bipolar spindle assembly in human cells. Using an “in vitro” evolution approach, we generated human cancer cells that can grow in the complete absence of Eg5 activity. Characterization of these Eg5-independent cells (EICs) led to the identification of a novel pathway for prophase centrosome separation, which depends on nuclear envelope (NE)-associated dynein. Here, we discuss our recent findings and elaborate on the mechanism by which dynein drives centrosome separation. |
format | Online Article Text |
id | pubmed-3656018 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-36560182013-05-24 Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation van Heesbeen, Roy G.H.P. Raaijmakers, Jonne A. Tanenbaum, Marvin E. Medema, René H. Commun Integr Biol Article Addendum Eg5 (kinesin-5) is a highly conserved microtubule motor protein, essential for centrosome separation and bipolar spindle assembly in human cells. Using an “in vitro” evolution approach, we generated human cancer cells that can grow in the complete absence of Eg5 activity. Characterization of these Eg5-independent cells (EICs) led to the identification of a novel pathway for prophase centrosome separation, which depends on nuclear envelope (NE)-associated dynein. Here, we discuss our recent findings and elaborate on the mechanism by which dynein drives centrosome separation. Landes Bioscience 2013-05-01 2013-05-01 /pmc/articles/PMC3656018/ /pubmed/23713137 http://dx.doi.org/10.4161/cib.23841 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Article Addendum van Heesbeen, Roy G.H.P. Raaijmakers, Jonne A. Tanenbaum, Marvin E. Medema, René H. Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation |
title | Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation |
title_full | Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation |
title_fullStr | Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation |
title_full_unstemmed | Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation |
title_short | Nuclear envelope-associated dynein cooperates with Eg5 to drive prophase centrosome separation |
title_sort | nuclear envelope-associated dynein cooperates with eg5 to drive prophase centrosome separation |
topic | Article Addendum |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3656018/ https://www.ncbi.nlm.nih.gov/pubmed/23713137 http://dx.doi.org/10.4161/cib.23841 |
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