Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1
The fundamental biophysics of gliding microtubule (MT) motility by surface-tethered kinesin-1 motor proteins has been widely studied, as well as applied to capture and transport analytes in bioanalytical microdevices. In these systems, phenomena such as molecular wear and fracture into shorter MTs h...
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Nature Publishing Group
2016
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5175155/ |
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pubmed-51751552016-12-28 Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 VanDelinder, Virginia Adams, Peter G. Bachand, George D. Article The fundamental biophysics of gliding microtubule (MT) motility by surface-tethered kinesin-1 motor proteins has been widely studied, as well as applied to capture and transport analytes in bioanalytical microdevices. In these systems, phenomena such as molecular wear and fracture into shorter MTs have been reported due the mechanical forces applied on the MT during transport. In the present work, we show that MTs can be split longitudinally into protofilament bundles (PFBs) by the work performed by surface-bound kinesin motors. We examine the properties of these PFBs using several techniques (e.g., fluorescence microscopy, SEM, AFM), and show that the PFBs continue to be mobile on the surface and display very high curvature compared to MT. Further, higher surface density of kinesin motors and shorter kinesin-surface tethers promote PFB formation, whereas modifying MT with GMPCPP or higher paclitaxel concentrations did not affect PFB formation. Nature Publishing Group 2016-12-21 /pmc/articles/PMC5175155/ /pubmed/28000714 http://dx.doi.org/10.1038/srep39408 Text en Copyright © 2016, The Author(s) 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 to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
VanDelinder, Virginia Adams, Peter G. Bachand, George D. |
| spellingShingle |
VanDelinder, Virginia Adams, Peter G. Bachand, George D. Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| author_facet |
VanDelinder, Virginia Adams, Peter G. Bachand, George D. |
| author_sort |
VanDelinder, Virginia |
| title |
Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| title_short |
Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| title_full |
Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| title_fullStr |
Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| title_full_unstemmed |
Mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| title_sort |
mechanical splitting of microtubules into protofilament bundles by surface-bound kinesin-1 |
| description |
The fundamental biophysics of gliding microtubule (MT) motility by surface-tethered kinesin-1 motor proteins has been widely studied, as well as applied to capture and transport analytes in bioanalytical microdevices. In these systems, phenomena such as molecular wear and fracture into shorter MTs have been reported due the mechanical forces applied on the MT during transport. In the present work, we show that MTs can be split longitudinally into protofilament bundles (PFBs) by the work performed by surface-bound kinesin motors. We examine the properties of these PFBs using several techniques (e.g., fluorescence microscopy, SEM, AFM), and show that the PFBs continue to be mobile on the surface and display very high curvature compared to MT. Further, higher surface density of kinesin motors and shorter kinesin-surface tethers promote PFB formation, whereas modifying MT with GMPCPP or higher paclitaxel concentrations did not affect PFB formation. |
| publisher |
Nature Publishing Group |
| publishDate |
2016 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5175155/ |
| _version_ |
1613807216962306048 |