Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail
Abstract Microtubules are major components of the eukaryotic cytoskeleton. Posttranslational modifications (PTMs) of tubulin regulates interactions with microtubule-associated proteins (MAPs). One unique PTM is the cyclical removal and re-addition of the C-terminal tyrosine of α-tubulin and MAPs con...
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-40425-4 |
| _version_ | 1797558218261528576 |
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| author | Xiangyu Fan Richard J. McKenney |
| author_facet | Xiangyu Fan Richard J. McKenney |
| author_sort | Xiangyu Fan |
| collection | DOAJ |
| description | Abstract Microtubules are major components of the eukaryotic cytoskeleton. Posttranslational modifications (PTMs) of tubulin regulates interactions with microtubule-associated proteins (MAPs). One unique PTM is the cyclical removal and re-addition of the C-terminal tyrosine of α-tubulin and MAPs containing CAP-Gly domains specifically recognize tyrosinated microtubules. KIF13B, a long-distance transport kinesin, contains a conserved CAP-Gly domain, but the role of the CAP-Gly domain in KIF13B’s motility along microtubules remains unknown. To address this, we investigate the interaction between KIF13B’s CAP-Gly domain, and tyrosinated microtubules. We find that KIF13B’s CAP-Gly domain influences the initial motor-microtubule interaction, as well as processive motility along microtubules. The effect of the CAP-Gly domain is enhanced when the motor domain is in the ADP state, suggesting an interplay between the N-terminal motor domain and C-terminal CAP-Gly domain. These results reveal that specialized kinesin tail domains play active roles in the initiation and continuation of motor movement. |
| first_indexed | 2024-03-10T17:28:13Z |
| format | Article |
| id | doaj.art-3ad89f0173034f789b975b3093079f86 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-10T17:28:13Z |
| publishDate | 2023-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-3ad89f0173034f789b975b3093079f862023-11-20T10:06:38ZengNature PortfolioNature Communications2041-17232023-08-0114111510.1038/s41467-023-40425-4Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tailXiangyu Fan0Richard J. McKenney1Department of Molecular and Cellular Biology, University of California - DavisDepartment of Molecular and Cellular Biology, University of California - DavisAbstract Microtubules are major components of the eukaryotic cytoskeleton. Posttranslational modifications (PTMs) of tubulin regulates interactions with microtubule-associated proteins (MAPs). One unique PTM is the cyclical removal and re-addition of the C-terminal tyrosine of α-tubulin and MAPs containing CAP-Gly domains specifically recognize tyrosinated microtubules. KIF13B, a long-distance transport kinesin, contains a conserved CAP-Gly domain, but the role of the CAP-Gly domain in KIF13B’s motility along microtubules remains unknown. To address this, we investigate the interaction between KIF13B’s CAP-Gly domain, and tyrosinated microtubules. We find that KIF13B’s CAP-Gly domain influences the initial motor-microtubule interaction, as well as processive motility along microtubules. The effect of the CAP-Gly domain is enhanced when the motor domain is in the ADP state, suggesting an interplay between the N-terminal motor domain and C-terminal CAP-Gly domain. These results reveal that specialized kinesin tail domains play active roles in the initiation and continuation of motor movement.https://doi.org/10.1038/s41467-023-40425-4 |
| spellingShingle | Xiangyu Fan Richard J. McKenney Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail Nature Communications |
| title | Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail |
| title_full | Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail |
| title_fullStr | Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail |
| title_full_unstemmed | Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail |
| title_short | Control of motor landing and processivity by the CAP-Gly domain in the KIF13B tail |
| title_sort | control of motor landing and processivity by the cap gly domain in the kif13b tail |
| url | https://doi.org/10.1038/s41467-023-40425-4 |
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