Kinesin-13s form rings around microtubules

Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving a...

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Autores principales: Tan, Dongyan, Asenjo, Ana B., Mennella, Vito, Sharp, David J., Sosa, Hernando
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064489/
https://www.ncbi.nlm.nih.gov/pubmed/17015621
http://dx.doi.org/10.1083/jcb.200605194
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author Tan, Dongyan
Asenjo, Ana B.
Mennella, Vito
Sharp, David J.
Sosa, Hernando
author_facet Tan, Dongyan
Asenjo, Ana B.
Mennella, Vito
Sharp, David J.
Sosa, Hernando
author_sort Tan, Dongyan
collection PubMed
description Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving along them. This depolymerization activity is important in mitosis during chromosome segregation. It is still not fully clear by which mechanism kinesin-13s depolymerize microtubules. To address this issue, we used electron microscopy to investigate the interaction of kinesin-13s with microtubules. Surprisingly, we found that proteins of the kinesin-13 family form rings and spirals around microtubules. This is the first report of this type of oligomeric structure for any kinesin protein. These rings may allow kinesin-13s to stay at the ends of microtubules during depolymerization.
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spelling pubmed-20644892007-11-29 Kinesin-13s form rings around microtubules Tan, Dongyan Asenjo, Ana B. Mennella, Vito Sharp, David J. Sosa, Hernando J Cell Biol Research Articles Kinesin is a superfamily of motor proteins that uses the energy of adenosine triphosphate hydrolysis to move and generate force along microtubules. A notable exception to this general description is found in the kinesin-13 family that actively depolymerizes microtubules rather than actively moving along them. This depolymerization activity is important in mitosis during chromosome segregation. It is still not fully clear by which mechanism kinesin-13s depolymerize microtubules. To address this issue, we used electron microscopy to investigate the interaction of kinesin-13s with microtubules. Surprisingly, we found that proteins of the kinesin-13 family form rings and spirals around microtubules. This is the first report of this type of oligomeric structure for any kinesin protein. These rings may allow kinesin-13s to stay at the ends of microtubules during depolymerization. The Rockefeller University Press 2006-10-09 /pmc/articles/PMC2064489/ /pubmed/17015621 http://dx.doi.org/10.1083/jcb.200605194 Text en Copyright © 2006, The Rockefeller University Press 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.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Tan, Dongyan
Asenjo, Ana B.
Mennella, Vito
Sharp, David J.
Sosa, Hernando
Kinesin-13s form rings around microtubules
title Kinesin-13s form rings around microtubules
title_full Kinesin-13s form rings around microtubules
title_fullStr Kinesin-13s form rings around microtubules
title_full_unstemmed Kinesin-13s form rings around microtubules
title_short Kinesin-13s form rings around microtubules
title_sort kinesin-13s form rings around microtubules
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064489/
https://www.ncbi.nlm.nih.gov/pubmed/17015621
http://dx.doi.org/10.1083/jcb.200605194
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