TY - JOUR TI - NuMA recruits dynein activity to microtubule minus-ends at mitosis AU - Hueschen, Christina L AU - Kenny, Samuel J AU - Xu, Ke AU - Dumont, Sophie A2 - Carter, Andrew P VL - 6 PY - 2017 DA - 2017/11/29 SP - e29328 C1 - eLife 2017;6:e29328 DO - 10.7554/eLife.29328 UR - https://doi.org/10.7554/eLife.29328 AB - To build the spindle at mitosis, motors exert spatially regulated forces on microtubules. We know that dynein pulls on mammalian spindle microtubule minus-ends, and this localized activity at ends is predicted to allow dynein to cluster microtubules into poles. How dynein becomes enriched at minus-ends is not known. Here, we use quantitative imaging and laser ablation to show that NuMA targets dynactin to minus-ends, localizing dynein activity there. NuMA is recruited to new minus-ends independently of dynein and more quickly than dynactin; both NuMA and dynactin display specific, steady-state binding at minus-ends. NuMA localization to minus-ends involves a C-terminal region outside NuMA’s canonical microtubule-binding domain and is independent of minus-end binders γ-TuRC, CAMSAP1, and KANSL1/3. Both NuMA’s minus-end-binding and dynein-dynactin-binding modules are required to rescue focused, bipolar spindle organization. Thus, NuMA may serve as a mitosis-specific minus-end cargo adaptor, targeting dynein activity to minus-ends to cluster spindle microtubules into poles. KW - Potorous tridactylus KW - mitosis KW - spindle KW - microtubule KW - dynein KW - minus-end JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -