التفاصيل البيبلوغرافية
| العنوان: |
Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin |
| المؤلفون: |
Singh, Sudhir K., Siegler, Nurit, Pandey, Himanshu, Yanir, Neta, Popov, Mary, Goldstein-Levitin, Alina, Sadan, Mayan, Debs, Garrett, Zarivach, Raz, Frank, Gabriel A., Kass, Itamar, Sindelar, Charles V., Zalk, Ran, Gheber, Larisa |
| المصدر: |
Science Advances ; volume 10, issue 6 ; ISSN 2375-2548 |
| بيانات النشر: |
American Association for the Advancement of Science (AAAS) |
| سنة النشر: |
2024 |
| مصطلحات موضوعية: |
Multidisciplinary |
| الوصف: |
Several kinesin-5 motors (kinesin-5s) exhibit bidirectional motility. The mechanism of such motility remains unknown. Bidirectional kinesin-5s share a long N-terminal nonmotor domain (NTnmd), absent in exclusively plus-end–directed kinesins. Here, we combined in vivo, in vitro, and cryo–electron microscopy (cryo-EM) studies to examine the impact of NTnmd mutations on the motor functions of the bidirectional kinesin-5, Cin8. We found that NTnmd deletion mutants exhibited cell viability and spindle localization defects. Using cryo-EM, we examined the structure of a microtubule (MT)-bound motor domain of Cin8, containing part of its NTnmd. Modeling and molecular dynamic simulations based on the cryo-EM map suggested that the NTnmd of Cin8 interacts with the C-terminal tail of β-tubulin. In vitro experiments on subtilisin-treated MTs confirmed this notion. Last, we showed that NTnmd mutants are defective in plus-end–directed motility in single-molecule and antiparallel MT sliding assays. These findings demonstrate that the NTnmd, common to bidirectional kinesin-5s, is critical for their bidirectional motility and intracellular functions. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| DOI: |
10.1126/sciadv.adi1367 |
| الإتاحة: |
https://doi.org/10.1126/sciadv.adi1367Test |
| رقم الانضمام: |
edsbas.E9D10214 |
| قاعدة البيانات: |
BASE |
