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J Cell Biol. 2017 Oct 2;216(10):3029-3039. doi: 10.1083/jcb.201704120. Epub 2017 Aug 31.

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

Author information

1
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, Scotland, UK.
2
Institut de Génétique et Développement de Rennes, Centre National de la Recherche Scientifique, UMR 6290, Université de Rennes, Rennes, France.
3
Chair of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
4
Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Japan.
5
Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, Scotland, UK h.ohkura@ed.ac.uk.

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.

PMID:
28860275
PMCID:
PMC5626551
DOI:
10.1083/jcb.201704120
[Indexed for MEDLINE]
Free PMC Article

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