• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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

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.

Pubmed ID: 17060449


  • Mori D
  • Yano Y
  • Toyo-oka K
  • Yoshida N
  • Yamada M
  • Muramatsu M
  • Zhang D
  • Saya H
  • Toyoshima YY
  • Kinoshita K
  • Wynshaw-Boris A
  • Hirotsune S


Molecular and cellular biology

Publication Data

January 14, 2007

Associated Grants

  • Agency: NINDS NIH HHS, Id: NS 41030

Mesh Terms

  • Adenosine Triphosphatases
  • Animals
  • Aurora Kinase A
  • Aurora Kinases
  • Carrier Proteins
  • Cell Movement
  • Centrosome
  • Fetal Proteins
  • HeLa Cells
  • Humans
  • Mice
  • Mice, Transgenic
  • Microtubule-Associated Proteins
  • Microtubules
  • Mitosis
  • Phosphorylation
  • Protein-Serine-Threonine Kinases
  • Ubiquitin