NDEL1 phosphorylation by Aurora-A kinase is essential for centrosomal maturation, separation, and TACC3 recruitment

Daisuke Mori, Yoshihisa Yano, Kazuhito Toyo-Oka, Noriyuki Yoshida, Masami Yamada, Masami Muramatsu, Dongwei Zhang, Hideyuki Saya, Yoko Y. Toyoshima, Kazuhisa Kinoshita, Anthony Wynshaw-Boris, Shinji Hirotsune

研究成果: Article査読

116 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)352-367
ページ数16
ジャーナルMolecular and Cellular Biology
27
1
DOI
出版ステータスPublished - 01-01-2007
外部発表はい

All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 細胞生物学

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