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First published online 13 July 2009
doi: 10.1242/jcs.048223

Journal of Cell Science 122, 2750-2759 (2009)
Published by The Company of Biologists 2009
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Research Article

FAM29A, a target of Plk1 regulation, controls the partitioning of NEDD1 between the mitotic spindle and the centrosomes

Hui Zhu1, Kayleen Fang1 and Guowei Fang1,2,*

1 Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA
2 Genentech, South San Francisco, CA 94080, USA

* Author for correspondence (e-mail: fang.guowei{at}gene.com)

Accepted 5 May 2009

We previously showed that FAM29A, a spindle-associated protein, promotes microtubule-dependent microtubule amplification through its interaction with and recruitment of NEDD1, the targeting subunit of the {gamma}-tubulin ring complex. We report here that FAM29A is regulated by Plk1, a kinase essential for spindle assembly and its bipolarity. Plk1, FAM29A and NEDD1 form three separate complexes in vivo, not one single complex. Plk1 recruits FAM29A to spindle microtubules, which, in turn, targets NEDD1 to the spindle. Plk1 also recruits NEDD1 to the centrosomes, probably through a Plk1-NEDD1 interaction, but this interaction does not contribute to targeting NEDD1 to the spindle. Altering intracellular levels of FAM29A changes the distribution of NEDD1 between the centrosomes and the spindle, indicating that FAM29A controls the partition of NEDD1 between these two mitotic structures. Thus, Plk1 promotes microtubule nucleation from the centrosomes through a FAM29A-independent pathway and from the spindle through a FAM29A-dependent pathway. FAM29A controls the relative contributions of these two pathways to microtubule polymerization during mitosis.

Key words: Plk1, FAM29A, NEDD1, Centrosome, Mitotic spindle, Microtubule amplification


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