R. Honda et al., 14-3-3-ZETA PROTEIN BINDS TO THE CARBOXYL HALF OF MOUSE WEE1 KINASE, Biochemical and biophysical research communications, 230(2), 1997, pp. 262-265
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. Recombinan
t 14-3-3 zeta was demonstrated to bind to weel kinase in vitro. The we
el kinase phosphorylated by cdc2 kinase also bound to 14-3-3 zeta prot
ein. 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 n
ecessary for the binding was tested by a two hybrid system expressing
different lengths of peptides derived from weel kinase. Both the entir
e 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 rem
ained to be elucidated in relation to the regulation of G2 to M phase
transition through weel kinase. (C) 1997 Academic Press