The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition
Autoinhibition ensures the proper spatiotemporal control of the kinesin-3 motor activity. Here, the authors present the full-length structure of kinesin-3 KLP-6 in an autoinhibited state and observe that all the internal domains entwine around the motor domain via a multilevel-lockdown mechanism.
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-32048-y |
| _version_ | 1811223050328211456 |
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| author | Wenjuan Wang Jinqi Ren Weiye Song Yong Zhang Wei Feng |
| author_facet | Wenjuan Wang Jinqi Ren Weiye Song Yong Zhang Wei Feng |
| author_sort | Wenjuan Wang |
| collection | DOAJ |
| description | Autoinhibition ensures the proper spatiotemporal control of the kinesin-3 motor activity. Here, the authors present the full-length structure of kinesin-3 KLP-6 in an autoinhibited state and observe that all the internal domains entwine around the motor domain via a multilevel-lockdown mechanism. |
| first_indexed | 2024-04-12T08:26:23Z |
| format | Article |
| id | doaj.art-4fdb859652504f3c902420b4b49714bf |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-12T08:26:23Z |
| publishDate | 2022-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-4fdb859652504f3c902420b4b49714bf2022-12-22T03:40:23ZengNature PortfolioNature Communications2041-17232022-07-0113111110.1038/s41467-022-32048-yThe architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibitionWenjuan Wang0Jinqi Ren1Weiye Song2Yong Zhang3Wei Feng4National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesKey Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesAutoinhibition ensures the proper spatiotemporal control of the kinesin-3 motor activity. Here, the authors present the full-length structure of kinesin-3 KLP-6 in an autoinhibited state and observe that all the internal domains entwine around the motor domain via a multilevel-lockdown mechanism.https://doi.org/10.1038/s41467-022-32048-y |
| spellingShingle | Wenjuan Wang Jinqi Ren Weiye Song Yong Zhang Wei Feng The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition Nature Communications |
| title | The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition |
| title_full | The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition |
| title_fullStr | The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition |
| title_full_unstemmed | The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition |
| title_short | The architecture of kinesin-3 KLP-6 reveals a multilevel-lockdown mechanism for autoinhibition |
| title_sort | architecture of kinesin 3 klp 6 reveals a multilevel lockdown mechanism for autoinhibition |
| url | https://doi.org/10.1038/s41467-022-32048-y |
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