A flipped ion pair at the dynein–microtubule interface is critical for dynein motility and ATPase activation

@inproceedings{Uchimura2015AFI,
  title={A flipped ion pair at the dynein–microtubule interface is critical for dynein motility and ATPase activation},
  author={Seiichi Uchimura and Takashi Fujii and Hiroko Takazaki and Rie Ayukawa and Yosuke Nishikawa and Itsushi Minoura and You Hachikubo and Genji Kurisu and Kazuo Sutoh and Takahide Kon and Keiichi Namba and Etsuko Muto},
  booktitle={The Journal of cell biology},
  year={2015}
}
Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis of signal transmission at the dynein-MT interface remains unclear. Scanning mutagenesis of tubulin identified two residues in α-tubulin, R403 and E416, that are critical for ATPase activation and… CONTINUE READING
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