beta-Catenin is a Nek2 substrate involved in centrosome separation.


Journal Article

beta-Catenin plays important roles in cell adhesion and gene transcription, and has been shown recently to be essential for the establishment of a bipolar mitotic spindle. Here we show that beta-catenin is a component of interphase centrosomes and that stabilization of beta-catenin, mimicking mutations found in cancers, induces centrosome splitting. Centrosomes are held together by a dynamic linker regulated by Nek2 kinase and its substrates C-Nap1 (centrosomal Nek2-associated protein 1) and Rootletin. We show that beta-catenin binds to and is phosphorylated by Nek2, and is in a complex with Rootletin. In interphase, beta-catenin colocalizes with Rootletin between C-Nap1 puncta at the proximal end of centrioles, and this localization is dependent on C-Nap1 and Rootletin. In mitosis, when Nek2 activity increases, beta-catenin localizes to centrosomes at spindle poles independent of Rootletin. Increased Nek2 activity disrupts the interaction of Rootletin with centrosomes and results in binding of beta-catenin to Rootletin-independent sites on centrosomes, an event that is required for centrosome separation. These results identify beta-catenin as a component of the intercentrosomal linker and define a new function for beta-catenin as a key regulator of mitotic centrosome separation.

Full Text

Duke Authors

Cited Authors

  • Bahmanyar, S; Kaplan, DD; Deluca, JG; Giddings, TH; O'Toole, ET; Winey, M; Salmon, ED; Casey, PJ; Nelson, WJ; Barth, AIM

Published Date

  • January 1, 2008

Published In

Volume / Issue

  • 22 / 1

Start / End Page

  • 91 - 105

PubMed ID

  • 18086858

Pubmed Central ID

  • 18086858

International Standard Serial Number (ISSN)

  • 0890-9369

Digital Object Identifier (DOI)

  • 10.1101/gad.1596308


  • eng

Conference Location

  • United States