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Article

  • The EMBO Journal (2006) 25, 5670 - 5682
  • doi:10.1038/sj.emboj.7601459

Published online: 30 November 2006

GSK-3bold beta-regulated interaction of BICD with dynein is involved in microtubule anchorage at centrosome

Katsumi Fumoto1, Casper C Hoogenraad2 and Akira Kikuchi1

  1. Department of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan
  2. Department of Neuroscience, Erasmus Medical Center, Rotterdam, The Netherlands

Correspondence to:

Akira Kikuchi, Department of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan. Tel.: +81 82 257 5130; Fax: +81 82 257 5134; E-mail: akikuchi@hiroshima-u.ac.jp

Received 22 June 2006; Accepted 24 October 2006

Microtubule arrays direct intracellular organization and define cellular polarity. Here, we show a novel function of glycogen synthase kinase-3beta (GSK-3beta) in the organization of microtubule arrays through the interaction with Bicaudal-D (BICD). BICD is known to form a complex with dynein–dynactin and to function in the intracellular vesicle trafficking. Our data revealed that GSK-3beta is required for the binding of BICD to dynein but not to dynactin. Knockdown of GSK-3beta or BICD reduced centrosomally focused microtubules and induced the mislocalization of centrosomal proteins. The unfocused microtubules in GSK-3beta knockdown cells were rescued by the expression of the dynein intermediate chain-BICD fusion protein. Microtubule regrowth assays showed that GSK-3beta and BICD are required for the anchoring of microtubules to the centrosome. These results imply that GSK-3beta may function in transporting centrosomal proteins to the centrosome by stabilizing the BICD1 and dynein complex, resulting in the regulation of a focused microtubule organization.

  • Keywords:

    • anchoring,
    • BICD,
    • centrosome,
    • GSK-3,
    • microtubule