Structural Characterization Of Human Protein Kinase CKI Epsilon

P. Houfková¹ , E. Brumovská¹, S. Trantírková¹, C. Modak², T. Doležal¹ and L. Trantírek¹

¹Laboratory Of Structural Biology, Faculty Of Biological Sciences, University Of South Bohemia, Branišovská 31, 370 05 České Budějovice, Czech Republic

² Developmental Biology Center and Department of Medicine, University of California-Irvine, Irvine, California, USA

e-mail: meriit@centrum.cz

Casein kinase I epsilon (CKIe) is a human homologue of Drosophila Disc overgrown (Dco). In case of mutations in the Dco, mutant larvae (Dco³) fail to arrest growth of imaginal discs when they reach their normal size and the discs grow continuously to several times the wild-type final size [1]. Moreover a remarkably high frequency of somatic mutations was found in CKIein breast cancer [2]. In this project we would like to identify proteins which form stable association with CKIe under in vivo conditions and characterize the topology of the CKIe complex. These investigations will provide a molecular basis for understanding of CKIe function and for design of drugs modulating CKIe activity.

Acknowledgement

This work was supported by Grant Agency of the Czech Republic (301/07/0814).

[1] V.A. Jursnich, S.E. Fraser, L.I. Held, J. Ryerse & P.J. Bryant, Dev. Biol., 140 (1990) 413-29.

[2] T.J. Fuja, F. Lin, K.E. Osann & P.J. Bryant, Cancer Res., 64 (2004) 942-51.