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 and Shinji Hirotsune ()
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Masami Yamada: Osaka City University, Graduate School of Medicine, Asahi-machi 1-4-3, Abeno, Osaka 545-8585, Japan
Kanako Kumamoto: Osaka City University, Graduate School of Medicine, Asahi-machi 1-4-3, Abeno, Osaka 545-8585, Japan
Shintaro Mikuni: Laboratory of Molecular Cell Dynamics, Faculty of Advanced Life Science, Hokkaido University, N21W11, Kita-Ku, Hokkaido, Sapporo 001-0021, Japan
Yoshiyuki Arai: Laboratory for Nanosystems Physiology, Research Institute for Electronic Sciences, Hokkaido University, N20W11, Kita-ku, Hokkaido, Sapporo 001-0020, Japan
Masataka Kinjo: Laboratory of Molecular Cell Dynamics, Faculty of Advanced Life Science, Hokkaido University, N21W11, Kita-Ku, Hokkaido, Sapporo 001-0021, Japan
Takeharu Nagai: Laboratory for Nanosystems Physiology, Research Institute for Electronic Sciences, Hokkaido University, N20W11, Kita-ku, Hokkaido, Sapporo 001-0020, Japan
Yoshikazu Tsukasaki: Laboratory for Comprehensive Bioimaging, Riken QBiC, Furuedai 6-2-3, Suita, Osaka 565-0874, Japan
Tomonobu M Watanabe: Laboratory for Comprehensive Bioimaging, Riken QBiC, Furuedai 6-2-3, Suita, Osaka 565-0874, Japan
Mitsuru Fukui: Laboratory of Statistics, Osaka City University Graduate School of Medicine, Asahi-machi 1-4-3 Abeno, Osaka 545-8585, Japan
Mingyue Jin: Osaka City University, Graduate School of Medicine, Asahi-machi 1-4-3, Abeno, Osaka 545-8585, Japan
Shiori Toba: Osaka City University, Graduate School of Medicine, Asahi-machi 1-4-3, Abeno, Osaka 545-8585, Japan
Shinji Hirotsune: Osaka City University, Graduate School of Medicine, Asahi-machi 1-4-3, Abeno, Osaka 545-8585, Japan

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract 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.

Date: 2013
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DOI: 10.1038/ncomms3033

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