Effect of the Neck Linker on Processive Stepping of Kinesin Motor
Kinesin motor protein, which is composed of two catalytic domains connected together by a long coiled-coil stalk via two flexible neck linkers (NLs), can step processively on a microtubule towards the plus end by hydrolyzing adenosine triphosphate (ATP) molecules. To understand what the role is that...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-01-01
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| Series: | Biophysica |
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| Online Access: | https://www.mdpi.com/2673-4125/3/1/4 |
| _version_ | 1827751033639534592 |
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| author | Ping Xie |
| author_facet | Ping Xie |
| author_sort | Ping Xie |
| collection | DOAJ |
| description | Kinesin motor protein, which is composed of two catalytic domains connected together by a long coiled-coil stalk via two flexible neck linkers (NLs), can step processively on a microtubule towards the plus end by hydrolyzing adenosine triphosphate (ATP) molecules. To understand what the role is that the NL plays in the processive stepping, the dynamics of the kinesin motor are studied theoretically here by considering the mutation or deletion of an N-terminal cover strand that contributes to the docking of the NL in kinesin-1, the extension of the NL in kinesin-1, the mutation of the NL in kinesin-1, the swapping of the NL of kinesin-2 with that of kinesin-1, the joining of the stalk and neck of Ncd that moves towards the minus end of MT to the catalytic domain of kinesin-1, the replacement of catalytic domain of kinesin-1 with that of Ncd, and so on. The theoretical results give a consistent and quantitative explanation of various available experimental results about the effects of these mutations on motor dynamics and, moreover, provide predicted results. Additionally, the processive motility of kinesin-6 MKLP2 without NL docking is also explained. The available experimental data about the effect of NL mutations on the dynamics of the bi-directional kinesin-5 Cin8 are also explained. The studies are critically implicative to the mechanism of the stepping of the kinesin motor. |
| first_indexed | 2024-03-11T06:52:48Z |
| format | Article |
| id | doaj.art-a83c64784210433e9a973611bcbc8da7 |
| institution | Directory Open Access Journal |
| issn | 2673-4125 |
| language | English |
| last_indexed | 2024-03-11T06:52:48Z |
| publishDate | 2023-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biophysica |
| spelling | doaj.art-a83c64784210433e9a973611bcbc8da72023-11-17T09:53:17ZengMDPI AGBiophysica2673-41252023-01-0131466810.3390/biophysica3010004Effect of the Neck Linker on Processive Stepping of Kinesin MotorPing Xie0Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaKinesin motor protein, which is composed of two catalytic domains connected together by a long coiled-coil stalk via two flexible neck linkers (NLs), can step processively on a microtubule towards the plus end by hydrolyzing adenosine triphosphate (ATP) molecules. To understand what the role is that the NL plays in the processive stepping, the dynamics of the kinesin motor are studied theoretically here by considering the mutation or deletion of an N-terminal cover strand that contributes to the docking of the NL in kinesin-1, the extension of the NL in kinesin-1, the mutation of the NL in kinesin-1, the swapping of the NL of kinesin-2 with that of kinesin-1, the joining of the stalk and neck of Ncd that moves towards the minus end of MT to the catalytic domain of kinesin-1, the replacement of catalytic domain of kinesin-1 with that of Ncd, and so on. The theoretical results give a consistent and quantitative explanation of various available experimental results about the effects of these mutations on motor dynamics and, moreover, provide predicted results. Additionally, the processive motility of kinesin-6 MKLP2 without NL docking is also explained. The available experimental data about the effect of NL mutations on the dynamics of the bi-directional kinesin-5 Cin8 are also explained. The studies are critically implicative to the mechanism of the stepping of the kinesin motor.https://www.mdpi.com/2673-4125/3/1/4molecular motorkinesinneck linkermechanochemistry |
| spellingShingle | Ping Xie Effect of the Neck Linker on Processive Stepping of Kinesin Motor Biophysica molecular motor kinesin neck linker mechanochemistry |
| title | Effect of the Neck Linker on Processive Stepping of Kinesin Motor |
| title_full | Effect of the Neck Linker on Processive Stepping of Kinesin Motor |
| title_fullStr | Effect of the Neck Linker on Processive Stepping of Kinesin Motor |
| title_full_unstemmed | Effect of the Neck Linker on Processive Stepping of Kinesin Motor |
| title_short | Effect of the Neck Linker on Processive Stepping of Kinesin Motor |
| title_sort | effect of the neck linker on processive stepping of kinesin motor |
| topic | molecular motor kinesin neck linker mechanochemistry |
| url | https://www.mdpi.com/2673-4125/3/1/4 |
| work_keys_str_mv | AT pingxie effectofthenecklinkeronprocessivesteppingofkinesinmotor |