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Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control
Molecular motors play critical roles in the formation of mitotic spindles, either through controlling the stability of individual microtubules, or by cross-linking and sliding microtubule arrays. Kinesin-8 motors are best known for their regulatory roles in controlling microtubule dynamics. They con...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3767134/ https://www.ncbi.nlm.nih.gov/pubmed/23851487 http://dx.doi.org/10.1038/ncb2801 |
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author | Su, Xiaolei Arellano-Santoyo, Hugo Portran, Didier Gaillard, Jeremie Vantard, Marylin Thery, Manuel Pellman, David |
author_facet | Su, Xiaolei Arellano-Santoyo, Hugo Portran, Didier Gaillard, Jeremie Vantard, Marylin Thery, Manuel Pellman, David |
author_sort | Su, Xiaolei |
collection | PubMed |
description | Molecular motors play critical roles in the formation of mitotic spindles, either through controlling the stability of individual microtubules, or by cross-linking and sliding microtubule arrays. Kinesin-8 motors are best known for their regulatory roles in controlling microtubule dynamics. They contain microtubule-destabilizing activities, and restrict spindle length in a wide variety of cell types and organisms. Here, we report for the first time on an anti-parallel microtubule-sliding activity of the budding yeast kinesin-8, Kip3. The in vivo importance of this sliding activity was established through the identification of complementary Kip3 mutants that separate the sliding activity and microtubule destabilizing activity. In conjunction with kinesin-5/Cin8, the sliding activity of Kip3 promotes bipolar spindle assembly and the maintenance of genome stability. We propose a “slide-disassemble” model where Kip3’s sliding and destabilizing activity balance during pre-anaphase. This facilitates normal spindle assembly. However, Kip3’s destabilizing activity dominates in late anaphase, inhibiting spindle elongation and ultimately promoting spindle disassembly. |
format | Online Article Text |
id | pubmed-3767134 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
spelling | pubmed-37671342014-02-01 Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control Su, Xiaolei Arellano-Santoyo, Hugo Portran, Didier Gaillard, Jeremie Vantard, Marylin Thery, Manuel Pellman, David Nat Cell Biol Article Molecular motors play critical roles in the formation of mitotic spindles, either through controlling the stability of individual microtubules, or by cross-linking and sliding microtubule arrays. Kinesin-8 motors are best known for their regulatory roles in controlling microtubule dynamics. They contain microtubule-destabilizing activities, and restrict spindle length in a wide variety of cell types and organisms. Here, we report for the first time on an anti-parallel microtubule-sliding activity of the budding yeast kinesin-8, Kip3. The in vivo importance of this sliding activity was established through the identification of complementary Kip3 mutants that separate the sliding activity and microtubule destabilizing activity. In conjunction with kinesin-5/Cin8, the sliding activity of Kip3 promotes bipolar spindle assembly and the maintenance of genome stability. We propose a “slide-disassemble” model where Kip3’s sliding and destabilizing activity balance during pre-anaphase. This facilitates normal spindle assembly. However, Kip3’s destabilizing activity dominates in late anaphase, inhibiting spindle elongation and ultimately promoting spindle disassembly. 2013-07-14 2013-08 /pmc/articles/PMC3767134/ /pubmed/23851487 http://dx.doi.org/10.1038/ncb2801 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Su, Xiaolei Arellano-Santoyo, Hugo Portran, Didier Gaillard, Jeremie Vantard, Marylin Thery, Manuel Pellman, David Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
title | Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
title_full | Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
title_fullStr | Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
title_full_unstemmed | Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
title_short | Microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
title_sort | microtubule sliding activity of a kinesin-8 promotes spindle assembly and spindle length control |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3767134/ https://www.ncbi.nlm.nih.gov/pubmed/23851487 http://dx.doi.org/10.1038/ncb2801 |
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