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Kinesin-8s hang on by a tail
Accurate segregation of genetic material into two daughter cells is essential for organism reproduction, development, and survival. The cell assembles a macromolecular structure called the mitotic spindle, which is composed of dynamic microtubules (MTs) and many associated proteins that assemble the...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384576/ https://www.ncbi.nlm.nih.gov/pubmed/22754615 http://dx.doi.org/10.4161/bioa.18427 |
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author | Weaver, Lesley N. Walczak, Claire |
author_facet | Weaver, Lesley N. Walczak, Claire |
author_sort | Weaver, Lesley N. |
collection | PubMed |
description | Accurate segregation of genetic material into two daughter cells is essential for organism reproduction, development, and survival. The cell assembles a macromolecular structure called the mitotic spindle, which is composed of dynamic microtubules (MTs) and many associated proteins that assemble the spindle and drive the segregation of the chromosomes. Members of the kinesin superfamily of MT associated proteins use the energy of ATP hydrolysis to help organize the spindle, to transport cargo within the spindle, and to regulate spindle MT dynamics. The Kinesin-8 and Kinesin-13 families are involved in controlling mitotic spindle morphology, spindle positioning, and chromosome movement. While both kinesin families are MT destabilizing enzymes, it is unclear whether their mechanisms of MT destabilization are mechanistically similar or how they act to destabilize MTs. Recently, three groups identified an additional MT binding domain within the tail of Kinesin-8s that is essential for their roles in regulating MT dynamics and chromosome positioning. |
format | Online Article Text |
id | pubmed-3384576 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-33845762012-06-29 Kinesin-8s hang on by a tail Weaver, Lesley N. Walczak, Claire Bioarchitecture Perspective Accurate segregation of genetic material into two daughter cells is essential for organism reproduction, development, and survival. The cell assembles a macromolecular structure called the mitotic spindle, which is composed of dynamic microtubules (MTs) and many associated proteins that assemble the spindle and drive the segregation of the chromosomes. Members of the kinesin superfamily of MT associated proteins use the energy of ATP hydrolysis to help organize the spindle, to transport cargo within the spindle, and to regulate spindle MT dynamics. The Kinesin-8 and Kinesin-13 families are involved in controlling mitotic spindle morphology, spindle positioning, and chromosome movement. While both kinesin families are MT destabilizing enzymes, it is unclear whether their mechanisms of MT destabilization are mechanistically similar or how they act to destabilize MTs. Recently, three groups identified an additional MT binding domain within the tail of Kinesin-8s that is essential for their roles in regulating MT dynamics and chromosome positioning. Landes Bioscience 2011-09-01 /pmc/articles/PMC3384576/ /pubmed/22754615 http://dx.doi.org/10.4161/bioa.18427 Text en Copyright © 2011 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 | Perspective Weaver, Lesley N. Walczak, Claire Kinesin-8s hang on by a tail |
title | Kinesin-8s hang on by a tail |
title_full | Kinesin-8s hang on by a tail |
title_fullStr | Kinesin-8s hang on by a tail |
title_full_unstemmed | Kinesin-8s hang on by a tail |
title_short | Kinesin-8s hang on by a tail |
title_sort | kinesin-8s hang on by a tail |
topic | Perspective |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384576/ https://www.ncbi.nlm.nih.gov/pubmed/22754615 http://dx.doi.org/10.4161/bioa.18427 |
work_keys_str_mv | AT weaverlesleyn kinesin8shangonbyatail AT walczakclaire kinesin8shangonbyatail |