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A new model for binding of kinesin 13 to curved microtubule protofilaments
Kinesin motor proteins use adenosine triphosphate hydrolysis to do work on microtubules (MTs). Most kinesins walk along the MT, but class 13 kinesins instead uniquely recognize MT ends and depolymerize MT protofilaments. We have used electron microscopy (EM) to understand the molecular interactions...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2700504/ https://www.ncbi.nlm.nih.gov/pubmed/19332892 http://dx.doi.org/10.1083/jcb.200812052 |
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author | Mulder, Anke M. Glavis-Bloom, Alex Moores, Carolyn A. Wagenbach, Michael Carragher, Bridget Wordeman, Linda Milligan, Ronald A. |
author_facet | Mulder, Anke M. Glavis-Bloom, Alex Moores, Carolyn A. Wagenbach, Michael Carragher, Bridget Wordeman, Linda Milligan, Ronald A. |
author_sort | Mulder, Anke M. |
collection | PubMed |
description | Kinesin motor proteins use adenosine triphosphate hydrolysis to do work on microtubules (MTs). Most kinesins walk along the MT, but class 13 kinesins instead uniquely recognize MT ends and depolymerize MT protofilaments. We have used electron microscopy (EM) to understand the molecular interactions by which kinesin 13 performs these tasks. Although a construct of only the motor domain of kinesin 13 binds to every heterodimer of a tubulin ring, a construct containing the neck and the motor domain occupies alternate binding sites. Likewise, EM maps of the dimeric full-length (FL) protein exhibit alternate site binding but reveal density for only one of two motor heads. These results indicate that the second head of dimeric kinesin 13 does not have access to adjacent binding sites on the curved protofilament and suggest that the neck alone is sufficient to obstruct access. Additionally, the FL construct promotes increased stacking of rings compared with other constructs. Together, these data suggest a model for kinesin 13 depolymerization in which increased efficiency is achieved by binding of one kinesin 13 molecule to adjacent protofilaments. |
format | Text |
id | pubmed-2700504 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27005042009-10-06 A new model for binding of kinesin 13 to curved microtubule protofilaments Mulder, Anke M. Glavis-Bloom, Alex Moores, Carolyn A. Wagenbach, Michael Carragher, Bridget Wordeman, Linda Milligan, Ronald A. J Cell Biol Research Articles Kinesin motor proteins use adenosine triphosphate hydrolysis to do work on microtubules (MTs). Most kinesins walk along the MT, but class 13 kinesins instead uniquely recognize MT ends and depolymerize MT protofilaments. We have used electron microscopy (EM) to understand the molecular interactions by which kinesin 13 performs these tasks. Although a construct of only the motor domain of kinesin 13 binds to every heterodimer of a tubulin ring, a construct containing the neck and the motor domain occupies alternate binding sites. Likewise, EM maps of the dimeric full-length (FL) protein exhibit alternate site binding but reveal density for only one of two motor heads. These results indicate that the second head of dimeric kinesin 13 does not have access to adjacent binding sites on the curved protofilament and suggest that the neck alone is sufficient to obstruct access. Additionally, the FL construct promotes increased stacking of rings compared with other constructs. Together, these data suggest a model for kinesin 13 depolymerization in which increased efficiency is achieved by binding of one kinesin 13 molecule to adjacent protofilaments. The Rockefeller University Press 2009-04-06 /pmc/articles/PMC2700504/ /pubmed/19332892 http://dx.doi.org/10.1083/jcb.200812052 Text en © 2009 Mulder et al. 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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Mulder, Anke M. Glavis-Bloom, Alex Moores, Carolyn A. Wagenbach, Michael Carragher, Bridget Wordeman, Linda Milligan, Ronald A. A new model for binding of kinesin 13 to curved microtubule protofilaments |
title | A new model for binding of kinesin 13 to curved microtubule protofilaments |
title_full | A new model for binding of kinesin 13 to curved microtubule protofilaments |
title_fullStr | A new model for binding of kinesin 13 to curved microtubule protofilaments |
title_full_unstemmed | A new model for binding of kinesin 13 to curved microtubule protofilaments |
title_short | A new model for binding of kinesin 13 to curved microtubule protofilaments |
title_sort | new model for binding of kinesin 13 to curved microtubule protofilaments |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2700504/ https://www.ncbi.nlm.nih.gov/pubmed/19332892 http://dx.doi.org/10.1083/jcb.200812052 |
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