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Published 6 June 2005. doi:10.1083/jcb.200410052
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 5, 719-724
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De novo formation of basal bodies in Naegleria gruberi

: regulation by phosphorylation



Hong-Kyung Kim1,2, Jeong-Gu Kang1,2, Shigehiko Yumura4, Charles J. Walsh5, Jin Won Cho1,2,3, and JooHun Lee1,2

1 Department of Biology, Yonsei University, Seoul 120-749, Korea
2 The Institute of Lifescience and Biotechnology, Yonsei University, Seoul 120-749, Korea
3 Protein Network Research Center, Yonsei University, Seoul 120-749, Korea
4 Department of Biology, Faculty of Science, Yamaguchi University, Yamaguchi 753- 8512, Japan
5 Department of Biological Sciences, University of Pittsburgh, PA 15260

Correspondence to JooHun Lee: leehjnt{at}yonsei.ac.kr; or Jin Won Cho: chojw311{at}yonsei.ac.kr


Abstract

The de novo formation of basal bodies in Naegleria gruberi was preceded by the transient formation of a microtubule (MT)-nucleating complex containing {gamma}-tubulin, pericentrin, and myosin II complex (GPM complex). The MT-nucleating activity of GPM complexes was maximal just before the formation of visible basal bodies and then rapidly decreased. The regulation of MT-nucleating activity of GPM complexes was accomplished by a transient phosphorylation of the complex. Inhibition of dephosphorylation after the formation of basal bodies resulted in the formation of multiple flagella. 2D-gel electrophoresis and Western blotting showed a parallel relationship between the MT-nucleating activity of GPM complexes and the presence of hyperphosphorylated {gamma}-tubulin in the complexes. These data suggest that the nucleation of MTs by GPM complexes precedes the de novo formation of basal bodies and that the regulation of MT-nucleating activity of GPM complexes is essential to the regulation of basal body number.

Abbreviations used in this paper: Ab, antibody; GPM complex, {gamma}-tubulin, pericentrin, and myosin II complex; MT, microtubule; PI, phosphatase inhibitors.


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