Molecular Mechanism of Processive Stepping of Kinesin Motors
Kinesin-1 is a motor protein that can step processively on microtubule by hydrolyzing ATP molecules, playing an essential role in intracellular transports. To better understand the mechanochemical coupling of the motor stepping cycle, numerous structural, biochemical, single molecule, theoretical mo...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-09-01
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| Series: | Symmetry |
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| Online Access: | https://www.mdpi.com/2073-8994/13/10/1799 |
| _version_ | 1797513106893570048 |
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| author | Ping Xie |
| author_facet | Ping Xie |
| author_sort | Ping Xie |
| collection | DOAJ |
| description | Kinesin-1 is a motor protein that can step processively on microtubule by hydrolyzing ATP molecules, playing an essential role in intracellular transports. To better understand the mechanochemical coupling of the motor stepping cycle, numerous structural, biochemical, single molecule, theoretical modeling and numerical simulation studies have been undertaken for the kinesin-1 motor. Recently, a novel ultraresolution optical trapping method was employed to study the mechanics of the kinesin-1 motor and new results were supplemented to its stepping dynamics. In this commentary, the new single molecule results are explained well theoretically with one of the models presented in the literature for the mechanochemical coupling of the kinesin-1 motor. With the model, various prior experimental results for dynamics of different families of N-terminal kinesin motors have also been explained quantitatively. |
| first_indexed | 2024-03-10T06:10:02Z |
| format | Article |
| id | doaj.art-02428417a2e94fd99b001e849ceb544b |
| institution | Directory Open Access Journal |
| issn | 2073-8994 |
| language | English |
| last_indexed | 2024-03-10T06:10:02Z |
| publishDate | 2021-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Symmetry |
| spelling | doaj.art-02428417a2e94fd99b001e849ceb544b2023-11-22T20:09:16ZengMDPI AGSymmetry2073-89942021-09-011310179910.3390/sym13101799Molecular Mechanism of Processive Stepping of Kinesin MotorsPing Xie0Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, ChinaKinesin-1 is a motor protein that can step processively on microtubule by hydrolyzing ATP molecules, playing an essential role in intracellular transports. To better understand the mechanochemical coupling of the motor stepping cycle, numerous structural, biochemical, single molecule, theoretical modeling and numerical simulation studies have been undertaken for the kinesin-1 motor. Recently, a novel ultraresolution optical trapping method was employed to study the mechanics of the kinesin-1 motor and new results were supplemented to its stepping dynamics. In this commentary, the new single molecule results are explained well theoretically with one of the models presented in the literature for the mechanochemical coupling of the kinesin-1 motor. With the model, various prior experimental results for dynamics of different families of N-terminal kinesin motors have also been explained quantitatively.https://www.mdpi.com/2073-8994/13/10/1799molecular motorkinesinmechanochemical coupling mechanism |
| spellingShingle | Ping Xie Molecular Mechanism of Processive Stepping of Kinesin Motors Symmetry molecular motor kinesin mechanochemical coupling mechanism |
| title | Molecular Mechanism of Processive Stepping of Kinesin Motors |
| title_full | Molecular Mechanism of Processive Stepping of Kinesin Motors |
| title_fullStr | Molecular Mechanism of Processive Stepping of Kinesin Motors |
| title_full_unstemmed | Molecular Mechanism of Processive Stepping of Kinesin Motors |
| title_short | Molecular Mechanism of Processive Stepping of Kinesin Motors |
| title_sort | molecular mechanism of processive stepping of kinesin motors |
| topic | molecular motor kinesin mechanochemical coupling mechanism |
| url | https://www.mdpi.com/2073-8994/13/10/1799 |
| work_keys_str_mv | AT pingxie molecularmechanismofprocessivesteppingofkinesinmotors |