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First published online October 22, 2008; 10.1104/pp.108.129346

Plant Physiology 148:1897-1907 (2008)
© 2008 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

Arabidopsis Casein Kinase 1-Like 6 Contains a Microtubule-Binding Domain and Affects the Organization of Cortical Microtubules1,[W],[OA]

Gili Ben-Nissan2,3, Weier Cui2, Dong-Jin Kim2, Yaodong Yang2, Byung-Chun Yoo and Jung-Youn Lee*

Department of Plant and Soil Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, Delaware 19711 (G.B.-N., W.C., D.-J.K., Y.Y., B.-C.Y., J.-Y.L.); and DuPont Crop Genetics Research, Experimental Station, Wilmington, Delaware 19880–0353 (B.-C.Y.)

Members of the casein kinase 1 (CK1) family are evolutionarily conserved eukaryotic protein kinases that are involved in various cellular, physiological, and developmental processes in yeast and metazoans, but the biological roles of CK1 members in plants are not well understood. Here, we report that an Arabidopsis (Arabidopsis thaliana) CK1 member named casein kinase 1-like 6 (CKL6) associates with cortical microtubules in vivo and phosphorylates tubulins in vitro. The unique C-terminal domain of CKL6 was shown to contain the signal that allows localization of CKL6 to the cortical microtubules. This domain on its own was sufficient to associate with microtubules in vivo and to bind tubulins in vitro. CKL6 was able to phosphorylate soluble tubulins as well as microtubule polymers, and its endogenous activity was found to associate with a tubulin-enriched subcellular fraction. Two major in vitro phosphorylation sites were mapped to serine-413 and serine-420 of tubulin β. Ectopic expression of wild-type CKL6 or a kinase-inactive mutant form induced alterations in cortical microtubule organization and anisotropic cell expansion. Collectively, these results demonstrate that CKL6 is a protein kinase containing a novel tubulin-binding domain and plays a role in anisotropic cell growth and shape formation in Arabidopsis through the regulation of microtubule organization, possibly through the phosphorylation of tubulins.


1 This work was supported by the National Science Foundation (grant no. MCB 0445626 to J.-Y.L.) and the National Institutes of Health (grant no. NCRR COBRE P20 RR–15588 to J.-Y.L.).

2 These authors contributed equally to the article.

3 Present address: Department of Biological Chemistry, Weizmann Institute of Science, 76100 Rehovot, Israel.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Jung-Youn Lee (lee{at}dbi.udel.edu).

[W] The online version of this article contains Web-only data.

[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.108.129346

* Corresponding author; e-mail lee{at}dbi.udel.edu.

Received September 5, 2008; accepted October 17, 2008; published October 22, 2008.




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A. Gokhale, M. Wirschell, and W. S. Sale
Regulation of dynein-driven microtubule sliding by the axonemal protein kinase CK1 in Chlamydomonas flagella
J. Cell Biol., September 21, 2009; 186(6): 817 - 824.
[Abstract] [Full Text] [PDF]




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