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Plant Physiology Preview Published on October 22, 2008; 10.1104/pp.108.129346
OPEN ACCESS ARTICLE
Received September 5, 2008 Arabidopsis Casein Kinase 1-Like 6 (CKL6) Contains Microtubule-Binding Domain and Affects Organization of Cortical Microtubules
Department of Plant and Soil Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, DE 19711, U. S. A; Crop Genetics, Agricultural Experimental Station, DuPont, Wilmington, DE 19880, U. S. A * Corresponding author; email: lee{at}dbi.udel.edu.
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 yeasts and metazoans, but the biological roles of CK1 members in plants are not well understood. Here we report that an Arabidopsis 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 Ser 413 and S420 of tubulin
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