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Microtubule teardrop patterns

Several strategies for controlling microtubule patterns are developed because of the rigidity determined from the molecular structure and the geometrical structure. In contrast to the patterns in co-operation with motor proteins or associated proteins, microtubules have a huge potential for patterns...

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Detalles Bibliográficos
Autores principales: Okeyoshi, Kosuke, Kawamura, Ryuzo, Yoshida, Ryo, Osada, Yoshihito
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4379470/
https://www.ncbi.nlm.nih.gov/pubmed/25823414
http://dx.doi.org/10.1038/srep09581
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author Okeyoshi, Kosuke
Kawamura, Ryuzo
Yoshida, Ryo
Osada, Yoshihito
author_facet Okeyoshi, Kosuke
Kawamura, Ryuzo
Yoshida, Ryo
Osada, Yoshihito
author_sort Okeyoshi, Kosuke
collection PubMed
description Several strategies for controlling microtubule patterns are developed because of the rigidity determined from the molecular structure and the geometrical structure. In contrast to the patterns in co-operation with motor proteins or associated proteins, microtubules have a huge potential for patterns via their intrinsic flexural rigidity. We discover that a microtubule teardrop pattern emerges via self-assembly under hydrodynamic flow from the parallel bundles without motor proteins. In the growth process, the bundles ultimately bend according to the critical bending curvature. Such protein pattern formation utilizing the intrinsic flexural rigidity will provide broad understandings of self-assembly of rigid rods, not only in biomolecules, but also in supramolecules.
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spelling pubmed-43794702015-04-07 Microtubule teardrop patterns Okeyoshi, Kosuke Kawamura, Ryuzo Yoshida, Ryo Osada, Yoshihito Sci Rep Article Several strategies for controlling microtubule patterns are developed because of the rigidity determined from the molecular structure and the geometrical structure. In contrast to the patterns in co-operation with motor proteins or associated proteins, microtubules have a huge potential for patterns via their intrinsic flexural rigidity. We discover that a microtubule teardrop pattern emerges via self-assembly under hydrodynamic flow from the parallel bundles without motor proteins. In the growth process, the bundles ultimately bend according to the critical bending curvature. Such protein pattern formation utilizing the intrinsic flexural rigidity will provide broad understandings of self-assembly of rigid rods, not only in biomolecules, but also in supramolecules. Nature Publishing Group 2015-03-31 /pmc/articles/PMC4379470/ /pubmed/25823414 http://dx.doi.org/10.1038/srep09581 Text en Copyright © 2015, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Okeyoshi, Kosuke
Kawamura, Ryuzo
Yoshida, Ryo
Osada, Yoshihito
Microtubule teardrop patterns
title Microtubule teardrop patterns
title_full Microtubule teardrop patterns
title_fullStr Microtubule teardrop patterns
title_full_unstemmed Microtubule teardrop patterns
title_short Microtubule teardrop patterns
title_sort microtubule teardrop patterns
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4379470/
https://www.ncbi.nlm.nih.gov/pubmed/25823414
http://dx.doi.org/10.1038/srep09581
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