Interaction of Aurora-A and centrosomin at the microtubule-nucleating site in Drosophila and mammalian cells

J Cell Biol. 2003 Sep 1;162(5):757-63. doi: 10.1083/jcb.200305048. Epub 2003 Aug 25.

Abstract

A mitosis-specific Aurora-A kinase has been implicated in microtubule organization and spindle assembly in diverse organisms. However, exactly how Aurora-A controls the microtubule nucleation onto centrosomes is unknown. Here, we show that Aurora-A specifically binds to the COOH-terminal domain of a Drosophila centrosomal protein, centrosomin (CNN), which has been shown to be important for assembly of mitotic spindles and spindle poles. Aurora-A and CNN are mutually dependent for localization at spindle poles, which is required for proper targeting of gamma-tubulin and other centrosomal components to the centrosome. The NH2-terminal half of CNN interacts with gamma-tubulin, and induces cytoplasmic foci that can initiate microtubule nucleation in vivo and in vitro in both Drosophila and mammalian cells. These results suggest that Aurora-A regulates centrosome assembly by controlling the CNN's ability to targeting and/or anchoring gamma-tubulin to the centrosome and organizing microtubule-nucleating sites via its interaction with the COOH-terminal sequence of CNN.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Nuclear / genetics
  • Antigens, Nuclear / metabolism*
  • Aurora Kinases
  • Cell Cycle Proteins / metabolism
  • Cell Line
  • Cricetinae
  • Drosophila / metabolism*
  • Microtubules / metabolism*
  • Protein Binding
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*
  • Protein Serine-Threonine Kinases
  • RNA Interference
  • Spindle Apparatus / metabolism
  • Tubulin / metabolism
  • Two-Hybrid System Techniques
  • Xenopus Proteins

Substances

  • Antigens, Nuclear
  • Cell Cycle Proteins
  • Tubulin
  • Xenopus Proteins
  • centrosomin A
  • Protein Kinases
  • AURKA protein, Xenopus
  • Aurora Kinases
  • Protein Serine-Threonine Kinases