14-3-3 regulation of Ncd reveals a new mechanism for targeting proteins to the spindle in oocytes

Abstract : The meiotic spindle is formed without centrosomes in a large volume of oocytes. Local activation of crucial spindle proteins around chromosomes is important for formation and maintenance of a bipolar spindle in oocytes. We found that phosphodocking 14-3-3 proteins stabilize spindle bipolarity in Drosophila melanogaster oocytes. A critical 14-3-3 target is the minus end-directed motor Ncd (human HSET; kinesin-14), which has well-documented roles in stabilizing a bipolar spindle in oocytes. Phospho docking by 14-3-3 inhibits the microtubule binding activity of the nonmotor Ncd tail. Further phosphorylation by Aurora B kinase can release Ncd from this inhibitory effect of 14-3-3. As Aurora B localizes to chromosomes and spindles, 14-3-3 facilitates specific association of Ncd with spindle microtubules by preventing Ncd from binding to nonspindle microtubules in oocytes. Therefore, 14-3-3 translates a spatial cue provided by Aurora B to target Ncd selectively to the spindle within the large volume of oocytes.
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Robin Beaven, Ricardo Nunes Bastos, Christos Spanos, Pierre Romé, C. Fiona Cullen, et al.. 14-3-3 regulation of Ncd reveals a new mechanism for targeting proteins to the spindle in oocytes. Journal of Cell Biology, Rockefeller University Press, 2017, 216 (10), pp.3029-3039. ⟨10.1083/jcb.201704120⟩. ⟨hal-01616455⟩

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