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Molecular and Cellular Biology, January 2007, p. 352-367, Vol. 27, No. 1
0270-7306/07/$08.00+0     doi:10.1128/MCB.00878-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

NDEL1 Phosphorylation by Aurora-A Kinase Is Essential for Centrosomal Maturation, Separation, and TACC3 Recruitment{triangledown} ,{dagger}

Daisuke Mori,1 Yoshihisa Yano,1 Kazuhito Toyo-oka,1 Noriyuki Yoshida,2 Masami Yamada,1 Masami Muramatsu,3 Dongwei Zhang,4 Hideyuki Saya,4 Yoko Y. Toyoshima,5 Kazuhisa Kinoshita,6 Anthony Wynshaw-Boris,7 and Shinji Hirotsune1,3*

Department of Genetic Disease Research,1 Department of Chemical Biology, Osaka City University Graduate School of Medicine, Asahi-machi 1-4-3 Abeno, Osaka 545-8586, Japan,2 Division of Neuro-Science, Research Center for Genomic Medicine, Saitama Medical School, Yamane 1397-1, Hidaka City, Saitama 350-1241, Japan,3 Department of Tumor Genetics and Biology, Graduate School of Medical Sciences, Kumamoto University, 1-1-1 Honjo, Kumamoto 860-8556, Japan,4 Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo 153-8902, Japan,5 Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany,6 Departments of Pediatrics and Medicine, Center for Human Genetics and Genomics, University of California, San Diego, School of Medicine, 9500 Gilman Drive, Mail Stop 0627, La Jolla, California 92093-06277

Received 17 May 2006/ Returned for modification 19 June 2006/ Accepted 12 September 2006

NDEL1 is a binding partner of LIS1 that participates in the regulation of cytoplasmic dynein function and microtubule organization during mitotic cell division and neuronal migration. NDEL1 preferentially localizes to the centrosome and is a likely target for cell cycle-activated kinases, including CDK1. In particular, NDEL1 phosphorylation by CDK1 facilitates katanin p60 recruitment to the centrosome and triggers microtubule remodeling. Here, we show that Aurora-A phosphorylates NDEL1 at Ser251 at the beginning of mitotic entry. Interestingly, NDEL1 phosphorylated by Aurora-A was rapidly downregulated thereafter by ubiquitination-mediated protein degradation. In addition, NDEL1 is required for centrosome targeting of TACC3 through the interaction with TACC3. The expression of Aurora-A phosphorylation-mimetic mutants of NDEL1 efficiently rescued the defects of centrosomal maturation and separation which are characteristic of Aurora-A-depleted cells. Our findings suggest that Aurora-A-mediated phosphorylation of NDEL1 is essential for centrosomal separation and centrosomal maturation and for mitotic entry.

* Corresponding author. Mailing address: Osaka City University Graduate School of Medicine, Genetic Disease Research, Asahi-machi 1-4-3 Abeno, Osaka 545-8586, Japan. Phone: 6-6645-3725. Fax: 6-6645-3727. E-mail: shinjih{at}med.osaka-cu.ac.jp.

{triangledown} Published ahead of print on 23 October 2006.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, January 2007, p. 352-367, Vol. 27, No. 1
0270-7306/07/$08.00+0     doi:10.1128/MCB.00878-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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