14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase

To identify proteins which bind to mouse weel kinase, the yeast ''two-hybrid'' system was used with a mouse cDNA library. Using the carboxyl half of weel kinase, the 14-3-3 zeta protein was isolated. Recombinant 14-3-3 zeta was demonstrated to bind to weel kinase in vitro. The weel kinase phosphorylated by cdc2 kinase also bound to 14-3-3 zeta protein. When both weel kinase and 14-3-3 zeta were transfected into COS-1 cells, they formed a complex in a cell. The sequence of weel kinase necessary for the binding was tested by a two hybrid system expressing different lengths of peptides derived from weel kinase. Both the entire kinase domain and a sequence in the carboxyl terminus was thought to be necessary for the binding. The function of 14-3-3 zeta protein remained to be elucidated in relation to the regulation of G2 to M phase transition through weel kinase. (C) 1997 Academic Press