Rab6a releases LIS1 from a dynein idling complex and activates dynein for retrograde movement

Masami Yamada, Kanako Kumamoto, Shintaro Mikuni, Yoshiyuki Arai, Masataka Kinjo, Takeharu Nagai, Yoshikazu Tsukasaki, Tomonobu M. Watanabe, Mitsuru Fukui, Mingyue Jin, Shiori Toba, Shinji Hirotsune

研究成果: ジャーナルへの寄稿学術論文査読

22 被引用数 (Scopus)


Cytoplasmic dynein drives the movement of a wide range of cargoes towards the minus ends of microtubules. We previously demonstrated that LIS1 forms an idling complex with dynein, which is transported to the plus ends of microtubules by kinesin motors. Here we report that the small GTPase Rab6a is essential for activation of idling dynein. Immunoprecipitation and microtubule pull-down assays reveal that the GTP bound mutant, Rab6a(Q72L), dissociates LIS1 from a LIS1-dynein complex, activating dynein movement in in vitro microtubule gliding assays. We monitor transient interaction between Rab6a(Q72L) and dynein in vivo using dual-colour fluorescence cross-correlation spectroscopy in dorsal root ganglion (DRG) neurons. Finally, we demonstrate that Rab6a(Q72L) mediates LIS1 release from a LIS1-dynein complex followed by dynein activation through an in vitro single-molecule assay using triple-colour quantum dots. Our findings reveal a surprising function for GTP bound Rab6a as an activator of idling dynein.

ジャーナルNature communications
出版ステータス出版済み - 2013

All Science Journal Classification (ASJC) codes

  • 化学一般
  • 生化学、遺伝学、分子生物学一般
  • 物理学および天文学一般


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