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TitleNoncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.
Journal, issue, pagesSci Adv, Vol. 10, Issue 6, Page eadi1367, Year 2024
Publish dateFeb 9, 2024
AuthorsSudhir K Singh / Nurit Siegler / Himanshu Pandey / Neta Yanir / Mary Popov / Alina Goldstein-Levitin / Mayan Sadan / Garrett Debs / Raz Zarivach / Gabriel A Frank / Itamar Kass / Charles V Sindelar / Ran Zalk / Larisa Gheber /
PubMed AbstractSeveral 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 ...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.
External linksSci Adv / PubMed:38324691 / PubMed Central
MethodsEM (helical sym.)
Resolution6.1 Å
Structure data

EMDB-10625:
Cin8 motor domain (short loop 8) bound to microtubules
Method: EM (helical sym.) / Resolution: 6.1 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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