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Kif18B interacts with EB1 and controls astral microtubule length during mitosis
Regulation of microtubule (MT) dynamics is essential for proper spindle assembly and organization. Kinesin-8 family members are plus-end-directed motors that modulate plus-end MT dynamics by acting as MT depolymerases or as MT plus-end capping proteins. In this paper, we show that the human kinesin-...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164455/ https://www.ncbi.nlm.nih.gov/pubmed/21737685 http://dx.doi.org/10.1091/mbc.E11-04-0363 |
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author | Stout, Jane R. Yount, Amber L. Powers, James A. LeBlanc, Chantal Ems-McClung, Stephanie C. Walczak, Claire E. |
author_facet | Stout, Jane R. Yount, Amber L. Powers, James A. LeBlanc, Chantal Ems-McClung, Stephanie C. Walczak, Claire E. |
author_sort | Stout, Jane R. |
collection | PubMed |
description | Regulation of microtubule (MT) dynamics is essential for proper spindle assembly and organization. Kinesin-8 family members are plus-end-directed motors that modulate plus-end MT dynamics by acting as MT depolymerases or as MT plus-end capping proteins. In this paper, we show that the human kinesin-8 Kif18B functions during mitosis to control astral MT organization. Kif18B is a MT plus-tip-tracking protein that localizes to the nucleus in interphase and is enriched at astral MT plus ends during early mitosis. Knockdown of Kif18B caused spindle defects, resulting in an increased number and length of MTs. A yeast two-hybrid screen identified an interaction of the C-terminal domain of Kif18B with the plus-end MT-binding protein EB1. EB1 knockdown disrupted Kif18B targeting to MT plus ends, indicating that EB1/Kif18B interaction is physiologically important. This interaction is direct, as the far C-terminal end of Kif18B is sufficient for binding to EB1 in vitro. Overexpression of this domain is sufficient for plus-end MT targeting in cells; however, targeting is enhanced by the motor domain, which cooperates with the tail to achieve proper Kif18B localization at MT plus ends. Our results suggest that Kif18B is a new MT dynamics regulatory protein that interacts with EB1 to control astral MT length. |
format | Online Article Text |
id | pubmed-3164455 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-31644552011-11-16 Kif18B interacts with EB1 and controls astral microtubule length during mitosis Stout, Jane R. Yount, Amber L. Powers, James A. LeBlanc, Chantal Ems-McClung, Stephanie C. Walczak, Claire E. Mol Biol Cell Articles Regulation of microtubule (MT) dynamics is essential for proper spindle assembly and organization. Kinesin-8 family members are plus-end-directed motors that modulate plus-end MT dynamics by acting as MT depolymerases or as MT plus-end capping proteins. In this paper, we show that the human kinesin-8 Kif18B functions during mitosis to control astral MT organization. Kif18B is a MT plus-tip-tracking protein that localizes to the nucleus in interphase and is enriched at astral MT plus ends during early mitosis. Knockdown of Kif18B caused spindle defects, resulting in an increased number and length of MTs. A yeast two-hybrid screen identified an interaction of the C-terminal domain of Kif18B with the plus-end MT-binding protein EB1. EB1 knockdown disrupted Kif18B targeting to MT plus ends, indicating that EB1/Kif18B interaction is physiologically important. This interaction is direct, as the far C-terminal end of Kif18B is sufficient for binding to EB1 in vitro. Overexpression of this domain is sufficient for plus-end MT targeting in cells; however, targeting is enhanced by the motor domain, which cooperates with the tail to achieve proper Kif18B localization at MT plus ends. Our results suggest that Kif18B is a new MT dynamics regulatory protein that interacts with EB1 to control astral MT length. The American Society for Cell Biology 2011-09-01 /pmc/articles/PMC3164455/ /pubmed/21737685 http://dx.doi.org/10.1091/mbc.E11-04-0363 Text en © 2011 Stout et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Stout, Jane R. Yount, Amber L. Powers, James A. LeBlanc, Chantal Ems-McClung, Stephanie C. Walczak, Claire E. Kif18B interacts with EB1 and controls astral microtubule length during mitosis |
title | Kif18B interacts with EB1 and controls astral microtubule length during mitosis |
title_full | Kif18B interacts with EB1 and controls astral microtubule length during mitosis |
title_fullStr | Kif18B interacts with EB1 and controls astral microtubule length during mitosis |
title_full_unstemmed | Kif18B interacts with EB1 and controls astral microtubule length during mitosis |
title_short | Kif18B interacts with EB1 and controls astral microtubule length during mitosis |
title_sort | kif18b interacts with eb1 and controls astral microtubule length during mitosis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3164455/ https://www.ncbi.nlm.nih.gov/pubmed/21737685 http://dx.doi.org/10.1091/mbc.E11-04-0363 |
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