Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin
Cargo transport within cells is essential to healthy cells, which requires microtubules-based motors, including kinesin. The C-terminal tails (E-hooks) of alpha and beta tubulins of microtubules have been proven to play important roles in interactions between the kinesins and tubulins. Here, we impl...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/4/2035 |
| _version_ | 1797479374708015104 |
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| author | Yixin Xie Lin Li |
| author_facet | Yixin Xie Lin Li |
| author_sort | Yixin Xie |
| collection | DOAJ |
| description | Cargo transport within cells is essential to healthy cells, which requires microtubules-based motors, including kinesin. The C-terminal tails (E-hooks) of alpha and beta tubulins of microtubules have been proven to play important roles in interactions between the kinesins and tubulins. Here, we implemented multi-scale computational methods in E-hook-related analyses, including flexibility investigations of E-hooks, binding force calculations at binding interfaces between kinesin and tubulins, electrostatic potential calculations on the surface of kinesin and tubulins. Our results show that E-hooks have several functions during the binding process: E-hooks utilize their own high flexibilities to increase the chances of reaching a kinesin; E-hooks help tubulins to be more attractive to kinesin. Besides, we also observed the differences between alpha and beta tubulins: beta tubulin shows a higher flexibility than alpha tubulin; beta tubulin generates stronger attractive forces (about twice the strengths) to kinesin at different distances, no matter with E-hooks in the structure or not. Those facts may indicate that compared to alpha tubulin, beta tubulin contributes more to attracting and catching a kinesin to microtubule. Overall, this work sheds the light on microtubule studies, which will also benefit the treatments of neurodegenerative diseases, cancer treatments, and preventions in the future. |
| first_indexed | 2024-03-09T21:44:57Z |
| format | Article |
| id | doaj.art-59d4a40cd8a84d2d96753a4ee3e531d0 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T21:44:57Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-59d4a40cd8a84d2d96753a4ee3e531d02023-11-23T20:18:50ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-02-01234203510.3390/ijms23042035Computational Study on E-Hooks of Tubulins in the Binding Process with KinesinYixin Xie0Lin Li1Computational Science Program, The University of Texas at El Paso, El Paso, TX 79912, USAComputational Science Program, The University of Texas at El Paso, El Paso, TX 79912, USACargo transport within cells is essential to healthy cells, which requires microtubules-based motors, including kinesin. The C-terminal tails (E-hooks) of alpha and beta tubulins of microtubules have been proven to play important roles in interactions between the kinesins and tubulins. Here, we implemented multi-scale computational methods in E-hook-related analyses, including flexibility investigations of E-hooks, binding force calculations at binding interfaces between kinesin and tubulins, electrostatic potential calculations on the surface of kinesin and tubulins. Our results show that E-hooks have several functions during the binding process: E-hooks utilize their own high flexibilities to increase the chances of reaching a kinesin; E-hooks help tubulins to be more attractive to kinesin. Besides, we also observed the differences between alpha and beta tubulins: beta tubulin shows a higher flexibility than alpha tubulin; beta tubulin generates stronger attractive forces (about twice the strengths) to kinesin at different distances, no matter with E-hooks in the structure or not. Those facts may indicate that compared to alpha tubulin, beta tubulin contributes more to attracting and catching a kinesin to microtubule. Overall, this work sheds the light on microtubule studies, which will also benefit the treatments of neurodegenerative diseases, cancer treatments, and preventions in the future.https://www.mdpi.com/1422-0067/23/4/2035E-hooksC-terminusmicrotubulesalpha tubulinbeta tubulinstructure flexibility |
| spellingShingle | Yixin Xie Lin Li Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin International Journal of Molecular Sciences E-hooks C-terminus microtubules alpha tubulin beta tubulin structure flexibility |
| title | Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin |
| title_full | Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin |
| title_fullStr | Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin |
| title_full_unstemmed | Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin |
| title_short | Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin |
| title_sort | computational study on e hooks of tubulins in the binding process with kinesin |
| topic | E-hooks C-terminus microtubules alpha tubulin beta tubulin structure flexibility |
| url | https://www.mdpi.com/1422-0067/23/4/2035 |
| work_keys_str_mv | AT yixinxie computationalstudyonehooksoftubulinsinthebindingprocesswithkinesin AT linli computationalstudyonehooksoftubulinsinthebindingprocesswithkinesin |