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



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 CKIein 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.



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.