Toyooka Lab

Translational Research for Autism & Parkinson's Disease

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


Journal article


D. Mori, Y. Yano, K. Toyo-oka, Noriyuki Yoshida, Masami Yamada, M. Muramatsu, Dongwei Zhang, H. Saya, Y. Toyoshima, K. Kinoshita, A. Wynshaw-Boris, S. Hirotsune
Molecular and Cellular Biology, vol. 27(1), 2006, pp. 352-367

Semantic Scholar DOI PubMed
Cite

Cite

APA   Click to copy
Mori, D., Yano, Y., Toyo-oka, K., Yoshida, N., Yamada, M., Muramatsu, M., … Hirotsune, S. (2006). NDEL1 Phosphorylation by Aurora-A Kinase Is Essential for Centrosomal Maturation, Separation, and TACC3 Recruitment. Molecular and Cellular Biology, 27(1), 352–367.


Chicago/Turabian   Click to copy
Mori, D., Y. Yano, K. Toyo-oka, Noriyuki Yoshida, Masami Yamada, M. Muramatsu, Dongwei Zhang, et al. “NDEL1 Phosphorylation by Aurora-A Kinase Is Essential for Centrosomal Maturation, Separation, and TACC3 Recruitment.” Molecular and Cellular Biology 27, no. 1 (2006): 352–367.


MLA   Click to copy
Mori, D., et al. “NDEL1 Phosphorylation by Aurora-A Kinase Is Essential for Centrosomal Maturation, Separation, and TACC3 Recruitment.” Molecular and Cellular Biology, vol. 27, no. 1, 2006, pp. 352–67.


BibTeX   Click to copy

@article{d2006a,
  title = {NDEL1 Phosphorylation by Aurora-A Kinase Is Essential for Centrosomal Maturation, Separation, and TACC3 Recruitment},
  year = {2006},
  issue = {1},
  journal = {Molecular and Cellular Biology},
  pages = {352-367},
  volume = {27},
  author = {Mori, D. and Yano, Y. and Toyo-oka, K. and Yoshida, Noriyuki and Yamada, Masami and Muramatsu, M. and Zhang, Dongwei and Saya, H. and Toyoshima, Y. and Kinoshita, K. and Wynshaw-Boris, A. and Hirotsune, S.}
}

Abstract

ABSTRACT 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.