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A number of polyclonal mouse sera were raised against Drosophila proteins that bound to microtubules in vitro (Kellogg et al. (1989) J. Cell Biol. 109, 2977-2991). Some of these sera recognised centrosomes in vivo, and we have been using these to screen expression libraries to isolate cDNAs encoding these putative centrosomal microtubule-associated proteins. Here we report the cloning of one such cDNA that encodes a novel serine/threonine protein kinase called LK6. The protein appears to exist in two forms: an abundant 185 kDa form and a rarer approximately 220 kDa form that interacts with microtubules. At least some of the LK6 protein is located in centrosomes at all stages of the cell cycle in fly embryos. Interestingly, the protein contains a PEST-like sequence and is rapidly turned over in vivo. Constitutive overexpression of LK6 is deleterious to flies and causes defects in microtubule organisation in both eggs and early embryos, whereas constitutive overexpression of a mutant form containing a point mutation that severely impairs the kinase activity is without effect. These findings suggest that LK6 may play a role in regulating microtubule function.


Journal article


J Cell Sci

Publication Date



110 ( Pt 2)


209 - 219


Amino Acid Sequence, Animals, Antibodies, Base Sequence, Centrosome, DNA, Complementary, Drosophila, Electrophoresis, Polyacrylamide Gel, Female, Insect Proteins, Microtubules, Molecular Sequence Data, Ovum, Phosphorylation, Protein Kinases, Protein-Serine-Threonine Kinases, Rabbits, Sequence Homology, Amino Acid, Sodium Dodecyl Sulfate, Time Factors