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Arl3 and LC8 regulate dissociation of dynactin from dynein

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  • Mingyue Jin

    (Osaka City University Graduate School of Medicine)

  • Masami Yamada

    (Osaka City University Graduate School of Medicine)

  • Yoshiyuki Arai

    (Institute of Scientific and Industrial Research, Osaka University)

  • Takeharu Nagai

    (Institute of Scientific and Industrial Research, Osaka University)

  • Shinji Hirotsune

    (Osaka City University Graduate School of Medicine)

Abstract

Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. However, the regulatory mechanism underlying release of dynactin bound cargoes from dynein motor remains largely unknown. Here we report that ADP-ribosylation factor-like 3 (Arl3) and dynein light chain LC8 induce dissociation of dynactin from dynein. Immunoprecipitation and microtubule pull-down assays revealed that Arl3(Q71L) and LC8 facilitated detachment of dynactin from dynein. We also demonstrated Arl3(Q71L) or LC8-mediated dynactin release from a dynein–dynactin complex through trace experiments using quantum dot (Qdot)-conjugated proteins. Furthermore, we disclosed interactions of Arl3 and LC8 with dynactin and dynein, respectively, by live-cell imaging. Finally, knockdown (KD) of Arl3 and LC8 by siRNA induced abnormal localizations of dynein, dynactin and related organelles. Our findings uncovered the surprising functional relevance of GTP-bound Arl3 and LC8 for the unloading regulation of dynactin-bound cargo from dynein motor.

Suggested Citation

  • Mingyue Jin & Masami Yamada & Yoshiyuki Arai & Takeharu Nagai & Shinji Hirotsune, 2014. "Arl3 and LC8 regulate dissociation of dynactin from dynein," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6295
    DOI: 10.1038/ncomms6295
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