Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules
Abstract Kinesin-14 microtubule-based motors have an N-terminal tail attaching the catalytic core to its load and usually move towards microtubule minus ends, whilst most other kinesins have a C-terminal tail and move towards plus ends. Loss of conserved sequences external to the motor domain causes...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2022-09-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-022-19589-4 |
| _version_ | 1811183773271719936 |
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| author | Masahiko Yamagishi Rieko Sumiyoshi Douglas R. Drummond Junichiro Yajima |
| author_facet | Masahiko Yamagishi Rieko Sumiyoshi Douglas R. Drummond Junichiro Yajima |
| author_sort | Masahiko Yamagishi |
| collection | DOAJ |
| description | Abstract Kinesin-14 microtubule-based motors have an N-terminal tail attaching the catalytic core to its load and usually move towards microtubule minus ends, whilst most other kinesins have a C-terminal tail and move towards plus ends. Loss of conserved sequences external to the motor domain causes kinesin-14 to switch to plus-end motility, showing that an N-terminal attachment is compatible with plus-end motility. However, there has been no systematic study on the role of attachment position in minus-end motility. We therefore examined the motility of monomeric kinesin-14s differing only in their attachment point. We find that a C-terminal attachment point causes kinesin-14s to become plus-end-directed, with microtubule corkscrewing rotation direction and pitch in motility assays similar to that of kinesin-1, suggesting that both C-kinesin kinesins-14 and N-kinesin kinesin-1 share a highly conserved catalytic core function with an intrinsic plus-end bias. Thus, an N-terminal attachment is one of the requirements for minus-end motility in kinesin-14. |
| first_indexed | 2024-04-11T09:52:37Z |
| format | Article |
| id | doaj.art-1cbcf47a6e204680a9334042a788893d |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-11T09:52:37Z |
| publishDate | 2022-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-1cbcf47a6e204680a9334042a788893d2022-12-22T04:30:45ZengNature PortfolioScientific Reports2045-23222022-09-0112111410.1038/s41598-022-19589-4Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubulesMasahiko Yamagishi0Rieko Sumiyoshi1Douglas R. Drummond2Junichiro Yajima3Department of Life Sciences, Graduate School of Arts and Sciences, The University of TokyoDepartment of Life Sciences, Graduate School of Arts and Sciences, The University of TokyoCentre for Promotion of International Education and Research, Faculty of Agriculture, Kyushu UniversityDepartment of Life Sciences, Graduate School of Arts and Sciences, The University of TokyoAbstract Kinesin-14 microtubule-based motors have an N-terminal tail attaching the catalytic core to its load and usually move towards microtubule minus ends, whilst most other kinesins have a C-terminal tail and move towards plus ends. Loss of conserved sequences external to the motor domain causes kinesin-14 to switch to plus-end motility, showing that an N-terminal attachment is compatible with plus-end motility. However, there has been no systematic study on the role of attachment position in minus-end motility. We therefore examined the motility of monomeric kinesin-14s differing only in their attachment point. We find that a C-terminal attachment point causes kinesin-14s to become plus-end-directed, with microtubule corkscrewing rotation direction and pitch in motility assays similar to that of kinesin-1, suggesting that both C-kinesin kinesins-14 and N-kinesin kinesin-1 share a highly conserved catalytic core function with an intrinsic plus-end bias. Thus, an N-terminal attachment is one of the requirements for minus-end motility in kinesin-14.https://doi.org/10.1038/s41598-022-19589-4 |
| spellingShingle | Masahiko Yamagishi Rieko Sumiyoshi Douglas R. Drummond Junichiro Yajima Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules Scientific Reports |
| title | Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules |
| title_full | Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules |
| title_fullStr | Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules |
| title_full_unstemmed | Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules |
| title_short | Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules |
| title_sort | anchoring geometry is a significant factor in determining the direction of kinesin 14 motility on microtubules |
| url | https://doi.org/10.1038/s41598-022-19589-4 |
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